WO2025119528A1 - Hair surface modification using special peptides - Google Patents

Abstract

The invention relates to methods for treating keratin fibers, said methods involving the use of agents (A) and (B). Agent (A) contains at least one peptide which comprises or consists of an amino acid sequence of 5 to 50 amino acids. The peptides are characterized by having, in an N- to C-terminus orientation, the amino acid sequence X₅X₆X₇X₈X₉, wherein each of the five groups X represents an amino acid of a particular group, and/or the amino acid sequence shares at least 85% sequence identity with one of the amino acid sequences mentioned in SEQ ID NOs: 1 - 17. Agent (B) contains at least one film-forming substance.

Description

Modification of the hair surface through special peptides

The present application relates to a method for treating keratin fibers, in particular human hair, comprising the application of agents (A) and (B). Agent (A) contains at least one peptide with a specific binding capacity to keratin fibers, which comprises or consists of an amino acid sequence of 5 to 50 amino acids. The peptides are characterized in that the amino acid residues at positions X5, Xe, X7, Xe, and Xg are each selected from a group of very specific amino acids, and/or that the peptides have a sequence identity of at least 85% with the amino acid sequences listed in SEQ ID NOs: 1-17. Agent (B) contains at least one film-forming substance.

A further subject matter of the present application is a multi-component packaging unit (kit of parts) which comprises the two agents (A) and (B) separately packaged in two containers.

In the field of hair cosmetics, the surface treatment of keratin fibers is a key topic. The defined deposition of substances on the surface of hair can, for example, increase its diameter and thus its volume; conditioning ingredients can form a barrier against external influences; or the formation of films can improve combability and manageability. In recent decades, a wide range of different substance classes have been used to specifically modify the hair surface, ranging from polymers to emulsifiers and cationic surfactants to monomeric active ingredients. As the topic of sustainability has recently become increasingly important, the current search is primarily for new compounds of biological origin. Adhesive peptides are of particular interest in this context because they are not only biodegradable, but as chains of linked amino acids, they also closely resemble the structure of keratin fibers.

Hair coloring processes in which coloring compounds are immobilized by forming films on the surface of hair are also increasingly at the center of current development work. Particularly important in this type of coloring process is the formation of uniform films that deliver consistent color results even on hair of different types or with varying degrees of damage. J. Cosmet. Sci. 62, 127-137 (March/April 2011) describes surface energy as an important physicochemical property of solid materials because it affects the surface properties of a solid, such as its wettability, the spreadability of substances on the surface, and their adhesive properties. The surface energy of hair influences how cosmetic compositions interact with the hair surface. It can be used to assess the condition of hair, as healthy hair always has a lower surface energy than damaged hair. All cosmetic products applied to the hair surface change the surface energy of the hair. For example, to improve the conditioning performance of the hair, the formulations should modify the surface of the treated hair, making it more hydrophobic, which reduces the surface energy. In connection with film-based dyeing processes, it has been found that a uniform deposition of film-forming materials on the hair surface occurs especially when all treated hair sections have the highest possible surface energy, ie when the surface of the fibers becomes as hydrophilic as possible.

The object of the present application was therefore to find a process that modifies the surface of keratin fibers or hair in such a way that their surface energy (alternatively also called "free surface energy" or "FSE" for short) is as high as possible and the surface of the fiber is thus as hydrophilic as possible. Such modification of the fibers should enable the formation of particularly uniform and homogeneous films on their surface. These films should form evenly on different hair types and hair with varying degrees of damage. When used in a coloring process, the resulting colored films should be bonded very permanently and evenly to the keratin fibers, deliver high color intensities, and have very good washfastness. Furthermore, a uniform and long-lasting color should be achieved both at the roots and in the hair tips. Furthermore, a uniform color result should be achieved on the keratin fibers or hair over their entire length, regardless of the degree of damage, and the film should remain on the fibers as evenly as possible over multiple hair washes, even on hair sections with varying degrees of damage.

The work leading to this invention has now shown that certain new peptides bind specifically to the surface of keratin or hair fibers and remain there for extended periods. By binding to the hair surface, such peptides can specifically alter the structure of the surface and thus influence its hydrophobicity or hydrophilicity. Because the fibers treated in this way have acquired a uniform degree of hydrophilicity across their entire surface, subsequently applied film-forming materials are deposited particularly evenly and homogeneously on the surface. A first subject of the present application is a method for treating keratin fibers, in particular human hair, comprising the following steps:

- application of an agent (A) to the keratin fibers, wherein the agent (A) contains at least one peptide comprising or consisting of an amino acid sequence of 5 to 50 amino acids, wherein

(Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence,

(X _a )nX ₅ X6X7X ₈ X9(Xb)m where each X _a is independently any amino acid, n is an integer from 0 to 45, preferably from 0 to 4,

X5 is an amino acid selected from the group consisting of P, H, T, N, R, C and A,

Xe is an amino acid selected from the group consisting of T, R, M, G, F, P, N, S, L, Y and W,

X7 is an amino acid selected from the group consisting of R, N, S, L, I, Q, W, G, A and Y,

Xe is an amino acid selected from the group consisting of K, T, N, A, L, F, D, R and G,

X9 is an amino acid selected from the group consisting of R, L, I, A, Q, P, H, G, W and M, each Xb is independently any amino acid, and m is an integer from 0 to 45, preferably from 0 to 7, particularly preferably from 0 to 3, and/or

(Ab) the amino acid sequence has at least 85%, preferably at least 86%, more preferably at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NOs: 1 - 17, and

- application of an agent (B) to the keratin fibers, wherein the agent (B) contains at least one film-forming substance.

Method for treating keratin fibers

The application of both agents (A) and (B) enables the formation of particularly uniform and durable films on the keratin fibers or hair. This formation of uniform films is advantageous in various keratin treatment procedures, such as styling or permanent fiber reshaping. However, it is particularly important in the dyeing process, since the films there are colored by incorporated coloring compounds and uneven removal then becomes particularly quickly visible.

The process for treating the keratin fibers can therefore be a process for coloring, temporarily reshaping, permanently reshaping or even for styling or caring for the keratin fibers.

Keratin fibers

Keratin fibers include hair, but also wool and fur. Human hair is particularly preferred as keratin fibers.

Medium (A)

The method according to the invention comprises the application of agent (A) to the keratin fibers or hair. Agent (A) is characterized in that it contains at least one specific peptide comprising or consisting of an amino acid sequence of 5 to 50 amino acids.

The agent (A) preferably contains the peptide(s) in a cosmetic carrier, particularly preferably in a suitable aqueous, alcoholic, or aqueous-alcoholic carrier. Such carriers can be, for example, creams, emulsions, gels, or surfactant-containing foaming solutions, such as shampoos, foam aerosols, foam formulations, or other preparations suitable for application to the hair.

Peptides

A peptide in the context of the present invention is understood to be a polymer composed of amino acids, preferably the 20 proteinogenic L-amino acids, preferably of linear structure, which comprises 5 to 50 amino acids linked to one another via peptide bonds. According to the invention, the peptides of the invention have an amino acid sequence of 5 to 50 amino acids. The amino acids are specified in the context of this invention in a one-letter code, where, for example, C stands for cysteine, R for arginine, A for alanine and L for leucine. It is further understood that, unless otherwise stated, the amino acids in an amino acid sequence disclosed herein are linked via peptide bonds and, unless otherwise stated, the sequence is listed in N- to C-terminal orientation.

The peptides of the invention can, in various embodiments, be chemically synthesized and/or produced recombinantly by protein design. Short peptides are now easily synthesized, for example, by solid-phase synthesis. Longer peptides and polypeptides, on the other hand, are often also produced recombinantly in the host organism. In the context of the present invention, the term “N-terminus” or “N-terminal” describes the end of the amino acid chain of the peptide according to the invention which has a free amino group.

In the context of the present invention, the term “C-terminus” or “C-terminal” describes the end of the amino acid chain of the peptide according to the invention which has a free carboxyl group.

The term “in N- to C-terminal orientation” in the context of this invention refers to an amino acid sequence in which the order of the amino acids is described from the N-terminus to the C-terminus.

Typical acidic or negatively charged amino acids (depending on the pH value) are D and E.

Positively charged or basic amino acids (depending on pH) typically include R, K and H.

Amino acids such as G, A, C, I, L, M, F, V, P, S, T, W, Y, N and Q are typically uncharged, i.e. neutral, amino acids.

When reference is made herein to an "any" amino acid, this typically means one of the 20 naturally occurring proteinogenic amino acids, i.e., one of glycine (G), alanine (A), valine (V), leucine (L), isoleucine (I), phenylalanine (F), serine (S), threonine (T), proline (P), methionine (M), cysteine (C), histidine (H), lysine (K), arginine (R), glutamine (Q), asparagine (N), aspartic acid (D), glutamic acid (E), tyrosine (Y), and tryptophan (W). The amino acids are typically L-amino acids unless otherwise stated. In alternative embodiments, the peptide may also consist of D-amino acids, although it may be preferred that D- and L-amino acids do not occur simultaneously within the peptides described herein.

The peptide(s) according to the invention comprise or consist of an amino acid sequence of 5 to 50 amino acids.

Peptides that consist of an amino acid sequence of 5 to 50 amino acids have a chain that is 5 to 50 amino acids long. Peptides that comprise an amino acid sequence of 5 to 50 amino acids have a chain of at least 5 amino acids to at least 50 amino acids, but can also have an even higher molecular weight and a chain that is more than 50 amino acids long. Preferably, the peptide has an amino acid sequence which has a length of 10 to 24 amino acids, for example 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23 or 24 amino acids, in particular 8 to 18 amino acids, most preferably 12 amino acids.

In principle, better adhesion to the hair surface was observed for the shorter peptides compared to the longer peptides. It is suspected that the defined sequence X5X6X7X8X9, or the positions directly adjacent to this sequence described below, is one of the sites through which the peptide interacts with specific positions or amino acid sequences on the hair surface. Thus, the adhesion to the hair surface increases with the larger the weight fraction of the interacting amino acids in relation to the total weight of the peptide.

Therefore, it is particularly preferred if the peptide according to the invention consists of an amino acid sequence of 5 to 50 amino acids, where

(a) the amino acid sequence in N- to C-terminal orientation has the following sequence, (X _a )nX ₅ X6X7X ₈ X9(Xb)m where each X _a is independently any amino acid, n is an integer from 0 to 45, preferably from 0 to 4,

X5 is an amino acid selected from the group consisting of P, H, T, N, R, C and A,

Xe is an amino acid selected from the group consisting of T, R, M, G, F, P, N, S, L, Y and W,

X7 is an amino acid selected from the group consisting of R, N, S, L, I, Q, W, G, A and Y,

Xe is an amino acid selected from the group consisting of K, T, N, A, L, F, D, R and G,

X9 is an amino acid selected from the group consisting of R, L, I, A, Q, P, H, G, W and M, each Xb is independently any amino acid, and m is an integer from 0 to 45, preferably from 0 to 7, more preferably from 0 to 3.

The invention relates to a peptide comprising or consisting of an amino acid sequence of 5 to 50 amino acids in length, preferably of at least 8, 9, 10, 11, or 12 amino acids in length. Preferred lengths are 8 to 40, preferably 9 to 35, more preferably 10 to 30, and particularly preferably 11 to 25 amino acids. For example, the peptide can also have a length of 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, or 24 amino acids, in particular 12 to 18 amino acids. Explicitly particularly preferably, the peptide consists of an amino acid sequence which has a length of 10 to 24 amino acids, for example 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23 or 24 amino acids, in particular 8 to 18 amino acids, very particularly preferably 12 amino acids.

For example, if the peptide comprises at least 5 amino acids, then in embodiment (a) it is characterized in that it has an amino acid sequence in N- to C-terminal orientation,

(X _a )nX ₅ X6X7X ₈ X9(Xb)m where n stands for the number 0, the residues X5, X6, X7, X8 and X9 each stand for an amino acid selected from the aforementioned specific groups, and m also stands for the number 0.

If the peptide consists of an amino acid sequence of 5 amino acids, then it consists of the above-mentioned chain of the 5 defined amino acids XsXeX XsXg.

If the peptide comprises at least 6 amino acids, then in embodiment (a) it is characterized in that it has an amino acid sequence in N- to C-terminal orientation, (X _a )nX ₅ X6X7X ₈ X9(Xb)m where n stands for the number 0 or 1, the residues X5, X6, X7, X8 and X9 each stand for an amino acid selected from the aforementioned specific groups, and m stands for the number 0 or 1, the sum of n + m being 1. The peptide then comprises either a residue Xa or a residue Xb. If the peptide consists of an amino acid sequence of 6 amino acids, then it consists of the above-mentioned chain of 6 defined amino acids, accordingly has or comprises the chain X _a X ₅ X ₆ X7X ₈ X9 or nX ₅ X6X7X ₈ X ₉ Xb

If the peptide comprises at least 50 amino acids, then in embodiment (a) it is characterized in that it has an amino acid sequence in N- to C-terminal orientation, (X _a )nX ₅ X6X7X ₈ X ₉ (Xb)m where n is an integer from 0 to 45, the residues X5, X6, X7, X8 and X9 each represent an amino acid selected from the aforementioned specific groups, and m is a number from 0 to 45, the sum of n + m being 45. The peptide then comprises a total of 45 residues Xa and Xb, each Xa and each Xb independently representing any amino acid. This means that the 45 amino acid residues are located before and/or after the sequence X5XeX7X ₈ X9.

Peptides, which comprise or consist of an amino acid sequence of 7 to 49 amino acids, are constructed in a similar way.

The residue Xa stands independently for any amino acid, ie Xa stands for example for an amino acid from the group of glycine (G), alanine (A), valine (V), leucine (L), Isoleucine (I), phenylalanine (F), serine (S), threonine (T), proline (P), methionine (M), cysteine (C), histidine (H), lysine (K), arginine (R), glutamine (Q), asparagine (N), aspartic acid (D), glutamic acid (E), tyrosine (Y) and tryptophan (W).

The index number n stands for an integer from 0 to 45. Preferably, n stands for an integer from 0 to 4. This means that, in front of the chain of amino acids X5X6X7X8X9 (i.e., towards the N-terminal end of the amino acid sequence), there is particularly preferably either no further amino acid or that 1 to 3 further amino acids are located there. If, for example, there are three further amino acids in front of the chain of amino acids XsXeX/XaXg, then the peptide comprises the sequence in N- to C-terminal orientation

X _a X _a X _a X ₅ X6X7X ₈ Xg(Xb)m

X5 is an amino acid selected from the group consisting of P (proline), H (histidine), T (threonine), N (asparagine), R (arginine), C (cysteine), and A (alanine). It has been found that peptides in which X5 is an amino acid selected from the group consisting of P, N, and C, particularly preferably P, have a particularly high substantivity to the surface of the keratin fiber.

The peptide contained in the agent (A) is therefore particularly preferably characterized in that its amino acid sequence (Aa) in N- to C-terminal orientation has the following sequence

(X _a )nX ₅ X6X7X ₈ Xg(Xb)m where

X5 is an amino acid selected from the group consisting of P, N, and C, particularly preferably P.

In a particularly preferred embodiment, a method according to the invention is characterized in that the peptide in the agent (A)

(Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence (X _a )nX ₅ X6X7X ₈ Xg(Xb)m where

X5 is an amino acid selected from the group consisting of P, N, and C, particularly preferably P.

Xe is an amino acid selected from the group consisting of T (threonine), R (arginine), M (methionine), G (glycine), F (phenylalanine), P (proline), N (asparagine), S (serine), L (leucine), Y (tyrosine) and W (tryptophan).

In this context, it was found that especially those peptides have a particularly high substantivity to the surface of the keratin fiber, where Xe is an amino acid, which is selected from the group consisting of T, R, M and P, preferably from the group consisting of T, R and M, particularly preferably from the group consisting of T and R.

In a particularly preferred embodiment, a peptide according to the invention is therefore characterized in that

(Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence

(X _a )nX ₅ X6X7X ₈ X9(Xb)m where

Xe is an amino acid selected from the group consisting of T, R, M and P, preferably from the group consisting of T, R and M, particularly preferably from the group consisting of T and R.

In a particularly preferred embodiment, a method according to the invention is characterized in that the peptide in the agent (A)

(Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence (X _a )nX ₅ X6X7X ₈ X9(Xb)m where

Xe is an amino acid selected from the group consisting of T, R, M and P, preferably from the group consisting of T, R and M, particularly preferably from the group consisting of T and R.

X7 is an amino acid selected from the group consisting of R (arginine), N (asparagine), S (serine), L (leucine), I (isoleucine), Q (glutamine), W (tryptophan), G (glycine), A (alanine) and Y (tyrosine).

If the amino acid sequence of the peptides at position X7 contained an amino acid from the group of R and L, particularly preferably R, the substantivity of the peptides to human hair was particularly high.

For this reason, a peptide according to the invention is characterized in a further particularly preferred embodiment in that

(a) the amino acid sequence in N- to C-terminal orientation has the following sequence (X _a )nX ₅ X6X7X ₈ X ₉ (Xb)m where

X7 is an amino acid selected from the group consisting of R and L, particularly preferably R.

In a further particularly preferred embodiment, a method according to the invention is characterized in that the peptide in the agent (A) (Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence

(X _a )nX ₅ X6X7X ₈ X9(Xb)m where

X7 is an amino acid selected from the group consisting of R and L, particularly preferably R.

_X8 is an amino acid selected from the group consisting of K (lysine), T (threonine), N (asparagine), A (alanine), L (leucine), F (phenylalanine), D (aspartic acid), R (arginine), and G (glycine). Particularly good results were obtained when Xs is an amino acid selected from the group consisting of K, T, N, and F, preferably from the group consisting of K, T, and N, particularly preferably from the group consisting of K and T.

In a further particularly preferred embodiment, a peptide according to the invention is characterized in that

(a) the amino acid sequence in N- to C-terminal orientation has the following sequence (X _a )nX ₅ X6X7X ₈ X9(Xb)m where

X ₈ is an amino acid selected from the group consisting of K, T, N and F, preferably from the group consisting of K, T and N, particularly preferably from the group consisting of K and T.

In a particularly preferred embodiment, a method according to the invention is characterized in that the peptide in the agent (A)

(Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence

(X _a )nX ₅ X6X7X ₈ X ₉ (Xb)m where

X ₈ is an amino acid selected from the group consisting of K, T, N and F, preferably from the group consisting of K, T and N, particularly preferably from the group consisting of K and T.

At position X9 there is an amino acid selected from the group consisting of R (arginine), L (leucine), I (isoleucine), A (alanine), Q (glutamine), P (proline), H (histidine), G (glycine) and W (tryptophan). If X9 stands for an amino acid selected from the group consisting of R, L, A and P, preferably from the group consisting of R, L and P, particularly preferably from the group consisting of R and L, most preferably R, a particularly good durability on hair strands was observed for the peptides according to the invention. In a further particularly preferred embodiment, a peptide according to the invention is characterized in that

(a) the amino acid sequence in N- to C-terminal orientation has the following sequence (X _a )nX ₅ X6X7X ₈ X9(Xb)m where

X9 is an amino acid selected from the group consisting of R, L, A and P, preferably from the group consisting of R, L and P, particularly preferably from the group consisting of R and L, most preferably R.

In a particularly preferred embodiment, a method according to the invention is characterized in that the peptide in the agent (A)

(Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence

(X _a )nX ₅ X6X7X ₈ X9(Xb)m where

X9 is an amino acid selected from the group consisting of R, L, A and P, preferably from the group consisting of R, L and P, particularly preferably from the group consisting of R and L, most preferably R.

The residue Xb stands independently for any amino acid, i.e. Xb stands, for example, for an amino acid from the group of glycine (G), alanine (A), valine (V), leucine (L), isoleucine (I), phenylalanine (F), serine (S), threonine (T), proline (P), methionine (M), cysteine (C), histidine (H), lysine (K), arginine (R), glutamine (Q), asparagine (N), aspartic acid (D), glutamic acid (E), tyrosine (Y) and tryptophan (W).

In a further embodiment, particularly preferred is a peptide comprising or consisting of an amino acid sequence of 5 to 50 amino acids, wherein

(a) the amino acid sequence in N- to C-terminal orientation has the following sequence, (X _a )nX ₅ X6X7X ₈ X ₉ (Xb)m where each X _a is independently any amino acid, n is an integer from 0 to 45, preferably from 0 to 4,

X5 is an amino acid selected from the group consisting of P, N, and C,

Xe is an amino acid selected from the group consisting of T, R, M and P,

X7 is an amino acid selected from the group consisting of R and L

X ₈ is an amino acid selected from the group consisting of K, T, N and F,

X9 is an amino acid selected from the group consisting of R, L, A and P, each Xb is independently any amino acid, and m is an integer from 0 to 45, preferably from 0 to 7, more preferably from 0 to 3. In a further embodiment, particularly preferred is a peptide comprising or consisting of an amino acid sequence of 5 to 50 amino acids, wherein

(a) the amino acid sequence in N- to C-terminal orientation has the following sequence, (X _a )nX ₅ X6X7X ₈ X9(Xb)m where each X _a is independently any amino acid, n is an integer from 0 to 45, preferably from 0 to 4, X5 represents the amino acid P,

Xe is an amino acid selected from the group consisting of T and R,

X7 stands for the amino acid R,

Xe is an amino acid selected from the group consisting of K and T, X9 is an amino acid selected from the group consisting of R and L, each Xb is independently any amino acid, and m is an integer from 0 to 45, preferably from 0 to 7, more preferably from 0 to 3.

The index number m stands for an integer from 0 to 45. Preferably, m stands for an integer from 0 to 7. Most preferably, m stands for an integer from 0 to 3. For example, if m stands for the number 3, this means that after the chain of amino acids X5X6X7X8X9 (i.e. towards the C-terminal end of the amino acid sequence) there are three further arbitrary amino acids, so that the peptide then comprises the sequence (X _a )nX5X6X7XsX9XbXbXb.

All of the aforementioned features can be implemented individually or in any combination. However, certain combinations of the aforementioned radicals and index numbers are particularly well suited to achieving the object of the invention and are therefore particularly preferred.

Of the peptides investigated for this invention, those peptides that have shown particularly good adhesion to human hair comprise an amino acid sequence of 7 to 16 amino acids, with at least one further specific amino acid located both before and after the sequence X5X6X7X8X9. The particularly preferred peptides in embodiment (a) have the following sequence in N- to C-terminal orientation: (Xa)nX ₄ X ₅ X6X7X8X9Xl0(Xb)m

This means that the amino acid at position X4 is no longer just any amino acid (Xa), but rather an amino acid X4 selected from the group consisting of R (arginine), S (serine), I (isoleucine), V (valine), H (histidine), F (phenylalanine), T (threonine), G (glycine), L (leucine), E (glutamic acid), Q (glutamine) and K (lysine). Furthermore, the amino acid at position X10 no longer represents any amino acid (Xb), but rather an amino acid X10 selected from the group consisting of I (isoleucine), K (lysine), S (serine), Q (glutamine), R (arginine), L (leucine), H (histidine), A (alanine), and F (phenylalanine). In this context, n preferably represents the number 0 to 3, particularly preferably the number 3, and m represents the number 0 to 6, particularly preferably the number 0 to 2, most preferably the number 2.

In a further particularly preferred embodiment, a peptide according to the invention in embodiment (a) is characterized in that

(a) the amino acid sequence in N- to C-terminal orientation has the following sequence (X _a )nX4X ₅ X6X7X ₈ X9Xl0(Xb)m where n is the number 0 to 3, preferably the number 3,

X4 is an amino acid selected from the group consisting of R, S, I, V, H, F, T, G, L, E, Q and K,

X10 is an amino acid selected from the group consisting of I, K, S, Q, R, L, H, A and F, and m is the number 0 to 6, preferably the number 0 to 2, particularly preferably the number 2.

In a further particularly preferred embodiment, a method according to the invention is characterized in that the agent (A) contains at least one peptide which comprises or consists of an amino acid sequence of 7 to 16 amino acids, wherein

(Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence

(X _a )nX4X ₅ X6X7X ₈ X9Xl0(Xb)m where n stands for the number 0 to 3, preferably for the number 3,

X4 is an amino acid selected from the group consisting of R, S, I, V, H, F, T, G, L, E, Q and K,

X10 is an amino acid selected from the group consisting of I, K, S, Q, R, L, H, A and F, and m is the number 0 to 6, preferably the number 0 to 2, particularly preferably the number 2.

The substantivity to human hair could be further increased if X4 is an amino acid selected from the group consisting of R, S, I, F and G, preferably from the group consisting of R, S, I and F, particularly preferably from the group consisting of R, S and I. It also had positive effects with regard to adhesion to human hair when X10 is an amino acid selected from the group consisting of I, K and R, preferably from the group consisting of I and K, particularly preferably K.

In a further particularly preferred embodiment, a peptide according to the invention in embodiment (a) is characterized in that

(Aa) its amino acid sequence in N- to C-terminal orientation has the following sequence

(X _a )nX4X ₅ X6X7X ₈ X9Xl0(Xb)m where

X4 is an amino acid selected from the group consisting of R, S, I, F and G, preferably from the group consisting of R, S, I and F, particularly preferably from the group consisting of R, S and I, and/or

X10 is an amino acid selected from the group consisting of I, K and R, preferably from the group consisting of I and K, particularly preferably I.

In a further particularly preferred embodiment, a method according to the invention is characterized in that the peptide in agent (A)

(Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence

(X _a )nX4X ₅ X6X7X ₈ X9Xl0(Xb)m where

X4 is an amino acid selected from the group consisting of R, S, I, F and G, preferably from the group consisting of R, S, I and F, particularly preferably from the group consisting of R, S and I, and/or

X10 is an amino acid selected from the group consisting of I, K and R, preferably from the group consisting of I and K, particularly preferably K.

Of the series of peptides investigated for this invention _, those peptides that have shown even better adhesion to human hair are those comprising an amino acid sequence of 9 to 16 amino acids, with at least one further specific amino acid located both before and after the sequence _{X4X5X8X7X8X9Xio} . The particularly preferred peptides in embodiment (a) have the following sequence in N- to C-terminal orientation: (X _a ) 0X3X4X5X6X7X3X9X10X11 (Xb)m.

This means that the amino acid at position X3 is no longer just any amino acid (Xa), but rather an amino acid X3 selected from the group consisting of P (proline), R (arginine), I (isoleucine), N (asparagine), C (cysteine), L (leucine), A (alanine), V (valine) and Q (glutamine). Furthermore, the amino acid at position Xu no longer represents any amino acid (Xb), but rather an amino acid Xu selected from the group consisting of K (lysine), R (arginine), I (isoleucine), N (asparagine), G (glycine), E (glutamic acid), V (valine), A (alanine), S (serine), and W (tryptophan). In this context, n preferably represents the number 0 to 2, preferably the number 2, and m represents the number 0 to 5, preferably the number 0 or 1, particularly preferably the number 1.

In a further particularly preferred embodiment, a peptide according to the invention in embodiment (a) is characterized in that

(Aa) its amino acid sequence in N- to C-terminal orientation has the following sequence

(Xa) 0X3X4X5X6X7X3X9X10X11 (Xb)m where n stands for the number 0 to 2, preferably for the number 2,

X3 is an amino acid selected from the group consisting of P, R, I, N, C, L, A,

V and Q,

X11 is an amino acid selected from the group consisting of K, R, I, N, G, E, V, A, S and W, and m is the number 0 to 5, preferably the number 0 or 1, particularly preferably the number 1.

In a further particularly preferred embodiment, a method according to the invention is characterized in that the agent (A) contains at least one peptide which comprises or consists of an amino acid sequence of 9 to 16 amino acids, wherein

(Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence

(Xa) 01X3X4X5X0X7X8X9X10X11 (Xb)m where n stands for the number 0 to 2, preferably for the number 2,

X3 is an amino acid selected from the group consisting of P, R, I, N, C, L, A,

V and Q,

X11 is an amino acid selected from the group consisting of K, R, I, N, G, E, V, A, S and W, and m is the number 0 to 5, preferably the number 0 or 1, particularly preferably the number 1. Particularly positive effects with regard to substantivity to the hair fiber were observed when X3 was an amino acid selected from the group consisting of P, R and N, preferably from the group consisting of P and R, most preferably R.

Also positive effects on adhesion to human hair were found when Xu was an amino acid selected from the group consisting of K and R, most preferably K.

In a further particularly preferred embodiment, a peptide according to the invention is characterized in that

(Aa) its amino acid sequence in N- to C-terminal orientation has the following sequence

(Xa) 0X3X4X5X6X7X3X9X10X11 (Xb)m where

X3 is an amino acid selected from the group consisting of P, R and N, preferably from the group consisting of P and R, most preferably P, and/or

X11 is an amino acid selected from the group consisting of K and R, most preferably K.

In a further particularly preferred embodiment, a method according to the invention is characterized in that the peptide in agent (A)

(Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence

(Xa) 01X3X4X5X6X7X3X9X10X11 (Xb)m where

X3 is an amino acid selected from the group consisting of P, R and N, preferably from the group consisting of P and R, most preferably R, and/or

X11 is an amino acid selected from the group consisting of K and R, most preferably K.

The very best results were obtained with peptides comprising an amino acid sequence of 12 amino acids, with the amino acid sequence (a) having the sequence X1X2X3X4X5X6X7X8X9X10X11X12 in the N- to C-terminal orientation. Here, the sequence X5X6X7X8X9 is preceded (i.e., toward the N-terminal end) by not four random amino acids, but rather by the defined amino acids X1X2X3X4. X3 and X4, as well as their preferred and particularly preferred embodiments, have already been defined.

Xi is an amino acid selected from the group consisting of Q (glutamine), R (arginine), H (histidine), N (asparagine), I (isoleucine), T (threonine), A (alanine), D (aspartic acid) and G (glycine). X2 is an amino acid selected from the group consisting of H (histidine), N (asparagine), M (methionine), S (serine), E (glutamic acid), W (tryptophan), P (proline), V (valine), A (alanine) and F (phenylalanine).

Behind (i.e., toward the C-terminal end) of the sequence X5X6X7X8X9, the peptide no longer contains any three amino acids, but rather the defined amino acids X10X11X12. X10 and Xu, as well as their preferred and particularly preferred embodiments, have already been defined previously.

X12 is an amino acid selected from the group consisting of P (proline), R (arginine), Q (glutamine), I (isoleucine), T (threonine), E (glutamic acid), N (asparagine), L (leucine), A (alanine) and G (glycine).

In a further particularly preferred embodiment, a peptide according to the invention is characterized in that

(a) its amino acid sequence in N- to C-terminal orientation has the following sequence

X1X2X3X4X5X6X7X8X9X10X11X12 where

Xi is an amino acid selected from the group consisting of Q, R, H, N, I, T, A, D and G, and

X2 is an amino acid selected from the group consisting of H, N, M, S, E, W, P, V, A and F, and

X12 is an amino acid selected from the group consisting of P, R, Q, I, T, E, N, L, A and G.

In a further particularly preferred embodiment, a method according to the invention is characterized in that the agent (A) contains at least one peptide which comprises or consists of an amino acid sequence of 12 amino acids, wherein

(Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence

X1X2X3X4X5X6X7X8X9X10X11X12 where

Xi is an amino acid selected from the group consisting of Q, R, H, N, I, T, A, D and G, and

X2 is an amino acid selected from the group consisting of H, N, M, S, E, W, P, V, A and F, and

X12 is an amino acid selected from the group consisting of P, R, Q, I, T, E, N, L, A and G. Particularly positive effects with regard to substantivity to the hair fiber were observed when Xi was an amino acid selected from the group consisting of Q, R, I and A, preferably from the group consisting of Q, R and I, particularly preferably from the group consisting of Q and I.

It also had positive effects with regard to the adhesion to human hair when X2 is an amino acid selected from the group consisting of H, N, S and P, preferably from the group consisting of H, N and S, particularly preferably from the group consisting of H and N.

Furthermore, good adhesion to the hair fiber was observed when X12 is an amino acid selected from the group consisting of P, R, Q and T, preferably from the group consisting of P, R and Q, particularly preferably from the group consisting of P and R.

In a further particularly preferred embodiment, a peptide according to the invention is characterized in that

(Aa) its amino acid sequence in N- to C-terminal orientation has the following sequence

X1X2X3X4X5X6X7X8X9X10X11X12 where

Xi is an amino acid selected from the group consisting of Q, R, I and A, preferably from the group consisting of Q, R and I, particularly preferably Q, and/or

X2 is an amino acid selected from the group consisting of H, N, S and P, preferably from the group consisting of H, N and S, particularly preferably N, and/or

X12 is an amino acid selected from the group consisting of P, R, Q and T, preferably from the group consisting of P, R and Q, particularly preferably Q.

In a further particularly preferred embodiment, a method according to the invention is characterized in that the peptide in agent (A)

(Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence

X1X2X3X4X5X6X7X8X9X10X11X12 where

Xi is an amino acid selected from the group consisting of Q, R, I and A, preferably from the group consisting of Q, R and I, particularly preferably Q, and/or

X2 is an amino acid selected from the group consisting of H, N, S and P, preferably from the group consisting of H, N and S, particularly preferably N, and/or

X12 is an amino acid selected from the group consisting of P, R, Q and T, preferably from the group consisting of P, R and Q, particularly preferably Q. Within the scope of embodiment (Ab), the peptide according to the invention comprises an amino acid sequence of 5 to 50 amino acids, or it consists of this amino acid sequence, wherein the amino acid sequence has at least 85%, preferably at least 86%, more preferably at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with one of the amino acid sequences mentioned in SEQ ID NOs: 1 - 17.

The peptide according to the invention preferably comprises or consists of an amino acid sequence which has at least 85%, preferably at least 86%, more preferably at least 87%, even more preferably at least 88%, even more preferably at least 89%, even more preferably at least 90%, even more preferably at least 91%, even more preferably at least 92%, even more preferably at least 93%, even more preferably at least 94%, even more preferably at least 95%, even more preferably at least 96%, even more preferably at least 97%, even more preferably at least 98%, even more preferably at least 99%, in particular 100% sequence identity with one of the following amino acid sequences: QHPRPTRKRIKP (SEQ ID No: 1), QNRSPRRRTRKRR (SEQ ID No: 2), QNRIPTRTRKKQ (SEQ ID No: 3), RNPIPMRNLKRQ (SEQ ID No: 4), HHRRHGRTIIIR (SEQ ID No: 5), HMISTMNAASRR (SEQ ID No: 6), RSIVTFSLRQNRC (SEQ ID No: 7), NERHNRRLQGRI (SEQ ID No: 8), ISNFNPRFPRRT (SEQ ID No: 9), TWRTRNLKISEE (SEQ ID No: 10), APNGCRLNAKRR (SEQ ID No: 11), HVCLRSIDHSVN (SEQ ID No: 12), RALRALQALQALEALC (SEQ ID No: 13), RALEALWRALEALC (SEQ ID No: 14), DHAQRYGAGHSG (SEQ ID No: 15), HFVKTPARWAWG (SEQ ID No: 16) and/or GHQGHWYGMFRA (SEQ ID No: 17).

The peptides with the amino acid sequences of SEQ ID NOs: 1-17 have demonstrated very good durability even on hair of different types and ethnic origins. However, particularly good results were obtained with certain amino acid sequences. The peptides according to one of SEQ ID NOs: 1-13, and even more preferably one of SEQ ID NOs: 1-3, 8, and 13, proved particularly suitable. The very best results were obtained with SEQ ID NO: 3.

In a further particularly preferred embodiment, a method according to the invention is characterized in that the agent (A) contains at least one peptide which comprises an amino acid sequence of 5 to 50 amino acids, or it consists of this amino acid sequence, wherein the amino acid sequence has at least 85%, preferably at least 86%, more preferably at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with one of the amino acid sequences mentioned in SEQ ID NOs: 1 - 13.

In a further very particularly preferred embodiment, a method according to the invention is characterized in that the agent (A) contains at least one peptide which comprises an amino acid sequence of 5 to 50 amino acids, or it consists of this amino acid sequence, wherein the amino acid sequence has at least 85%, preferably at least 86%, more preferably at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with one of the amino acid sequences mentioned in SEQ ID NOs: 1-3, 8 and 13.

In a further particularly preferred embodiment, a method according to the invention is characterized in that the agent (A) contains at least one peptide which comprises an amino acid sequence of 5 to 50 amino acids, or it consists of this amino acid sequence, wherein the amino acid sequence comprises at least 85%, preferably at least 86%, more preferably at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% has sequence identity with one of the amino acid sequences listed in SEQ ID NOs: 1, 3, 8 and 13.

In the explicitly most preferred embodiment, a method according to the invention is characterized in that the agent (A) contains at least one peptide which comprises an amino acid sequence of 5 to 50 amino acids, or it consists of this amino acid sequence, wherein the amino acid sequence has at least 85%, preferably at least 86%, more preferably at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with the amino acid sequence mentioned in SEQ ID No: 3.

In a further particularly preferred embodiment, a method according to the invention is characterized in that the agent (A) contains at least one peptide which comprises or consists of an amino acid sequence of 5 to 50 amino acids, wherein

(Ab) the amino acid sequence has at least 85%, preferably at least 86%, more preferably at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with one of the amino acid sequences mentioned in SEQ ID NOs: 1 - 13, preferably with one of the amino acid sequences mentioned in SEQ ID Nos: 1-3, 8 and 13 and very particularly preferably with the amino acid sequence mentioned in SEQ ID No: 3.

Depending on the desired extent of surface coverage, the peptide(s) according to the invention can be present in agent (A) in various amounts. Agent (A) preferably contains—based on the total weight of agent (A)—one or more peptides according to the invention in a total amount of 0.0001 to 20 wt.%, preferably 0.01 to 15 wt.%, more preferably 0.1 to 10 wt.%, and most preferably 0.2 to 7.5 wt.%.

Determination of amino acid sequences

The determination of the identity of amino acid sequences can be achieved, for example, by sequence comparison. This sequence comparison is based on the state-of-the-art and commonly used BLAST algorithm (see, for example, Altschul, SF, Gish, W., Miller, W., Myers, EW & Lipman, DJ (1990) "Basic local alignment search tool." J. Mol. Biol. 215:403-410, and Altschul, Stephan F., Thomas L. Madden, Alejandro A. Schaffer, Jinghui Zhang, Hheng Zhang, Webb Miller, and David J. Lipman (1997): "Gapped BLAST and PSI-BLAST: a new generation of protein database search programs"; Nucleic Acids Res., 25, pp. 3389-3402) and is essentially performed by identifying similar sequences of nucleotides or amino acids in the Nucleic acid or amino acid sequences are assigned to one another. A tabular assignment of the relevant positions is called an alignment. Another algorithm available in the state of the art is the FASTA algorithm. Sequence comparisons (alignments), especially multiple sequence comparisons, are created using computer programs. Frequently used programs include the Clustal series (see, for example, Chenna et al. (2003): Multiple sequence alignment with the Clustal series of programs. Nucleic Acid Research 31 , 3497-3500), T-Coffee (see, for example, Notredame et al. (2000): T-Coffee: A novel method for multiple sequence alignments. J. Mol. Biol. 302, 205-217) or programs based on these programs or algorithms. Furthermore, sequence comparisons (alignments) are possible using the computer program Vector NTIR Suite 10.3 (Invitrogen Corporation, 1600 Faraday Avenue, Carlsbad, California, USA) with the specified default parameters. The AlignX module for sequence comparisons is based on ClustalW. Unless otherwise stated, the sequence identity stated herein is determined using the BLAST algorithm.

Such a comparison also allows a statement to be made about the similarity of the compared sequences. This is usually expressed as percent identity, i.e., the proportion of identical nucleotides or amino acid residues at the same or corresponding positions in an alignment. The broader term "homology" in amino acid sequences includes conserved amino acid substitutions, i.e., amino acids with similar chemical activity, since these usually exert similar chemical activities within the peptide/protein. Therefore, the similarity of the compared sequences can also be expressed as percent homology or percent similarity. Identity and/or homology statements can be made for entire peptides, polypeptides, or genes, or just for individual regions. Homologous or identical regions of different nucleic acid or amino acid sequences are therefore defined by similarities in the sequences. Such regions often exhibit identical functions. They can be small and comprise only a few nucleotides or amino acids. However, such small regions often perform essential functions for the overall activity of the peptide/protein. It may therefore be useful to refer sequence matches only to individual, possibly small, regions. Unless otherwise stated, however, statements of identity or homology in this application refer to the entire length of the respective amino acid sequence.

The peptide or protein concentration can be determined using known methods, for example the BCA method (bicinchoninic acid; 2,2'-biquinolyl-4,4'-dicarboxylic acid) or the biuret method (AG Gornall, CS Bardawill and MM David, J. Biol. Chem., 177 (1948), pp. 751-766). Those skilled in the art of peptide and protein technology are familiar with a variety of suitable methods for determining peptide or protein concentration that can be applied within the scope of this invention. Peptides according to the invention may contain amino acid modifications, particularly amino acid substitutions, insertions, or deletions. Such peptides are further developed, for example, through targeted genetic modification, i.e., through mutagenesis techniques, and optimized for specific applications or with regard to specific properties (e.g., with regard to their stability, binding, etc.).

For example, targeted mutations such as substitutions, insertions, or deletions can be introduced into known molecules to alter certain properties. For this purpose, the surface charges and/or the isoelectric point of the molecules, and thus their interactions with a surface, can be altered. For example, the net charge of the peptides can be altered to influence substrate binding. Alternatively or additionally, one or more corresponding mutations can increase, for example, the stability or adsorption of the peptide. Advantageous properties of individual mutations, e.g., individual substitutions, can complement each other.

The following convention is used to describe substitutions that affect exactly one amino acid position (amino acid exchanges): first, the naturally occurring amino acid is named using the internationally used one-letter code, followed by the corresponding sequence position and finally the inserted amino acid. Multiple exchanges within the same peptide chain are separated by slashes. In the case of insertions, additional amino acids are named after the sequence position. In the case of deletions, the missing amino acid is replaced by a symbol, such as an asterisk or a dash, or an A is indicated in front of the corresponding position. For example, P9T describes the substitution of proline at position 9 with threonine, P9TH the insertion of histidine after the amino acid threonine at position 9 and P9* or AP9 the deletion of proline at position 9. This nomenclature is familiar to those skilled in the art in the field of enzyme technology.

Thus, the invention also encompasses peptides which are characterized in that they are obtainable from a peptide as described above as the starting molecule, for example from a molecule with one of the amino acid sequences according to SEQ ID NOs: 1-17, preferably according to one of SEQ ID NOs 1-11, particularly preferably according to one of SEQ ID NOs: 1-4, 9 and 11, on which, for example, one or more amino acid substitutions, including single or multiple conservative amino acid substitutions, have been carried out, the resulting peptide having at least 85% sequence identity with one of the amino acid sequences according to SEQ ID NOs: 1-17, preferably 1-11, particularly preferably 1-4, 9 and 11.

The term "conservative amino acid substitution" means the exchange (substitution) of one amino acid residue for another amino acid residue, whereby this exchange does not lead to a change in the polarity or charge at the position of the exchanged amino acid, e.g. Exchange of one nonpolar amino acid residue for another nonpolar amino acid residue. Conservative amino acid substitutions within the scope of the invention include, for example: G=A=S, I=V=L=M, D=E, N=Q, K=R, Y=F, S=T, G=A=I=V=L=M=Y=F=W=P=S=T. However, it may be preferred that such exchanges do not have glycine or tyrosine as the target amino acid, or, for example, an amino acid that has a low alpha-helix-forming potential.

In preferred embodiments, the peptide of the invention can also be modified. Preferred modifications can, for example, be the coupling of the peptide of the invention with certain other molecules or chemical groups, for example, organic (macro)molecules, e.g., via a covalent bond or a linker via a suitable amino acid of the chain and/or N- and/or C-terminal.

If the peptide of the invention is coupled to at least one other (macro)molecule, it can also be referred to as a peptide derivative. The peptide of the invention is then derivatized. In such embodiments, the peptide can act as an adhesion tag, which causes the binding of a molecule coupled to it to the desired surface. Such molecules can also be referred to as conjugates.

In some embodiments, the said peptides according to the invention, which may, for example, have the amino acid cysteine N- or C-terminally for coupling purposes, are coupled with biotin (functionally modified), preferably at a suitable amino acid of the chain and/or N- and/or C-terminally.

Production of the peptides

The peptides according to the invention can be chemically prepared by known methods of peptide synthesis, for example by solid-phase synthesis according to Merrifield.

However, it is preferred to produce the peptides according to the invention using recombinant processes. According to the invention, this refers to all genetic engineering or microbiological processes based on the introduction of the genes for the peptides of interest into a host organism suitable for production and their transcribing and translating by this host organism (collectively referred to as biotechnological processes within the scope of this invention). For example, the genes in question are introduced via vectors, in particular expression vectors; but also via those that allow the gene of interest to be inserted into an already existing genetic element in the host organism, such as the chromosome or other vectors. The functional unit consisting of gene and promoter, and possibly other genetic elements, is typically referred to as an expression cassette. However, it does not necessarily have to be present as a physical unit. The peptides according to the invention are particularly preferably produced as polypeptides (multimers) and subsequently cleaved into the functional peptides. Very particularly preferred multimers have 2 to 10 peptide units (each according to the invention), which are each separated from one another by spacers of 0 to 4 amino acids in length (for example 1, 2, 3 or 4 amino acids). These spacers can consist, for example, of the amino acids glycine (G), alanine (A) and serine (S). Alternatively, the spacers can also be or comprise cleavage sites for specific proteases/peptidases, in particular endopeptidases, or can form such cleavage sites together with parts of the peptide according to the invention.

Using methods that are generally known today, such as chemical synthesis or the polymerase chain reaction (PCR) in conjunction with standard molecular biological and/or protein chemical methods, it is possible for a person skilled in the art to produce the corresponding nucleic acids up to complete genes based on known DNA and/or amino acid sequences and then to use these for the synthesis of peptides and polypeptides in suitable host cells.

In particularly preferred embodiments, the peptide is produced by biotechnological methods as defined above.

For the purposes of the present invention, vectors are understood to be elements consisting of nucleic acids that contain a gene of interest as a characteristic nucleic acid region. They are capable of establishing this gene in a species or cell line over several generations or cell divisions as a stable genetic element that replicates independently of the rest of the genome. Vectors, particularly when used in bacteria, are special plasmids, i.e., circular genetic elements. In genetic engineering, a distinction is made between vectors that serve for storage and thus, to a certain extent, also for genetic engineering work, the so-called cloning vectors, and those that fulfill the function of implementing the gene of interest in the host cell, i.e., enabling the expression of the relevant peptide. These vectors are referred to as expression vectors.

The nucleic acid encoding a peptide according to the invention or a multimer of such a peptide, which constitutes a further aspect of the invention, can, for example, be cloned into a vector. The molecular biological dimension of the invention thus consists in vectors with the genes for the corresponding peptides. These can include, for example, vectors derived from bacterial plasmids, viruses, or bacteriophages, or predominantly synthetic vectors or plasmids with elements of various origins. With the additional genetic elements present, vectors are capable of establishing themselves as stable units in the respective host cells over several generations. It is irrelevant for the purposes of the invention whether they establish themselves extrachromosomally as separate units or into a chromosome. Which of the numerous systems known from the state of the art is chosen depends on the individual case. Decisive factors may include, for example, the achievable copy number, the available selection systems, especially antibiotic resistance, or the culturability of host cells capable of taking up the vectors.

The vectors provide suitable starting points for molecular biological and biochemical studies of the gene in question or associated peptide, for further developments according to the invention, and ultimately for the amplification and production of peptides according to the invention. They represent further aspects of the present invention.

Preferred embodiments of the present invention are cloning vectors. In addition to storage, biological amplification, or selection of the gene of interest, these vectors are suitable for characterizing the gene in question, for example, by creating a restriction map or sequencing. Cloning vectors are also preferred embodiments of the present invention because they represent a transportable and storable form of the claimed DNA. They are also preferred starting points for molecular biological techniques that are not cell-dependent, such as the polymerase chain reaction.

Expression vectors are chemically similar to cloning vectors, but differ in those partial sequences that enable them to replicate in host organisms optimized for peptide production and to express the contained gene there. Preferred embodiments are expression vectors that themselves carry the genetic elements necessary for expression. Expression is influenced, for example, by promoters that regulate gene transcription. Thus, expression can occur through the natural promoter originally located upstream of this gene, but also after genetic fusion, both through a promoter of the host cell provided on the expression vector or through a modified or completely different promoter from another organism.

Preferred embodiments are those expression vectors that can be regulated by changes in the culture conditions or addition of certain compounds, such as cell density or specific factors.

Embodiments of the present invention may also be cell-free expression systems in which peptide biosynthesis is reproduced in vitro. Such expression systems are also established in the prior art. The in vivo synthesis of a peptide according to the invention, i.e., by living cells, requires the transfer of the corresponding gene into a host cell, known as its transformation. In principle, all organisms are suitable as host cells, i.e., prokaryotes, eukaryotes, or cyanophyta. Preferred host cells are those that are genetically easy to handle, for example, with regard to transformation with the expression vector and its stable establishment, such as unicellular fungi such as yeasts or bacteria. Furthermore, preferred host cells are characterized by good microbiological and biotechnological handling. This includes, for example, easy culturability, high growth rates, low requirements for fermentation media, and good production and secretion rates for foreign peptides. Often, the optimal expression systems for the individual case must be determined experimentally from the wealth of different systems available according to the state of the art. Each peptide according to the invention can be obtained from a variety of host organisms in this way.

A further aspect of the present invention relates to such host cells. Preferred embodiments are host cells whose activity can be regulated by genetic regulatory elements, which are provided, for example, on the expression vector, but can also be present in these cells from the outset. These cells can be stimulated to express, for example, by the controlled addition of chemical compounds that serve as activators, by changing the cultivation conditions, or upon reaching a certain cell density. This enables very economical production of the peptides of interest.

Preferred host cells are prokaryotic or bacterial cells. Bacteria are generally characterized by shorter generation times and lower demands on cultivation conditions compared to eukaryotes. This allows for the establishment of cost-effective processes for obtaining peptides according to the invention. In Gram-negative bacteria, such as E. coli, a large number of peptides are secreted into the periplasmic space, i.e., the compartment between the two membranes surrounding the cells. This can be advantageous for specific applications. Gram-positive bacteria, such as Bacilli or Actinomycetes or other members of the Actinomycetales, in contrast, do not have an outer membrane, so secreted peptides are immediately released into the nutrient medium surrounding the cells, from which, according to another preferred embodiment, the expressed peptides according to the invention can be directly purified.

A variation of this principle is represented by expression systems in which additional genes, for example those provided on other vectors, influence the production of peptides according to the invention. These can be modifying gene products or gene products that are to be co-purified with the peptide according to the invention. Due to the extensive experience gained, for example, with regard to molecular biological methods and cultivability with coliform bacteria, these represent preferred embodiments of the present invention. Particularly preferred are those of the genera Escherichia coli, in particular non-pathogenic strains suitable for biotechnological production.

Representative representatives of these genera are the K12 derivatives and the B strains of Escherichia coli. Strains that can be derived from these using known genetic and/or microbiological methods and can thus be regarded as their derivatives. These are of the greatest importance for genetic and microbiological work and are preferably used for the development of the methods according to the invention. Such derivatives can, for example, be modified via deletion or insertion mutagenesis with regard to their culture requirements, have different or additional selection markers, or express different or additional peptides. In particular, these can be derivatives that express other economically interesting peptides in addition to the peptide produced according to the invention.

Also preferred are microorganisms characterized by the fact that they have been obtained after transformation with one of the vectors described above. These can, for example, be cloning vectors that have been introduced into any bacterial strain for storage and/or modification. Such steps are common in the storage and further development of relevant genetic elements. Since the relevant genetic elements can be directly transferred from these microorganisms into Gram-negative bacteria suitable for expression, the preceding transformation products also represent realizations of the relevant subject matter of the invention.

Eukaryotic cells can also be suitable for producing peptides according to the invention. Examples include fungi such as Actinomycetes or yeasts such as Saccharomyces or Kluyveromyces. This can be particularly advantageous, for example, if the peptides are to undergo specific modifications during their synthesis that enable such systems. This includes, for example, the binding of low-molecular-weight compounds such as membrane anchors or oligosaccharides. In the context of this invention, this would be an example of a functionally modified peptide.

The host cells of the process according to the invention are cultivated and fermented in a conventional manner, for example, in discontinuous or continuous systems. In the first case, a suitable nutrient medium is inoculated with the recombinant bacterial strains, and the product is harvested from the medium after a period to be determined experimentally. Continuous fermentations are characterized by reaching a steady state in which cells partially die but also regrow over a comparatively long period of time and at the same time product can be removed from the medium.

Fermentation processes are well known in the art and represent the actual large-scale production step; followed by a suitable purification method.

All fermentation processes based on one of the above-described processes for producing the recombinant peptides represent correspondingly preferred embodiments of this subject matter of the invention.

In this case, the optimal conditions for the production processes used, for the host cells and/or the peptides to be produced must be determined experimentally on the basis of the previously optimized culture conditions of the strains in question according to the knowledge of the person skilled in the art, for example with regard to fermentation volume, media composition, oxygen supply or stirrer speed.

Fermentation processes characterized by a feed-in strategy are also possible. In this case, the media components consumed during continuous cultivation are added; this is also referred to as a supplementary feeding strategy. This can achieve significant increases in both cell density and dry biomass, and/or, above all, the activity of the peptide of interest.

Analogously, the fermentation can also be designed in such a way that undesirable metabolic products are filtered out or neutralized by adding buffer or appropriate counterions.

The produced peptide can be subsequently harvested from the fermentation medium. This fermentation process is preferred over product preparation from dry matter, but requires the provision of suitable secretion markers and transport systems.

Without secretion, purification of the peptide from the cell mass may be necessary. Various methods are known for this, such as precipitation, e.g., with ammonium sulfate or ethanol, or chromatographic purification, if necessary to homogeneity. However, the majority of the described technical methods should be sufficient with an enriched, stabilized preparation. All of the elements already outlined above can be combined into processes for producing peptides according to the invention. These processes for producing the peptides according to the invention represent further aspects of the present invention. A multitude of possible combinations of process steps are conceivable for each peptide according to the invention. Optimal conditions can be determined experimentally for each specific case.

Free surface energy

As previously described, the surface energy of keratin fibers or hair influences how cosmetic compositions interact with the fiber surface during application. Surface energy can be used to assess hair condition, as healthy hair always has a lower surface energy than damaged hair. All cosmetic products applied to the hair surface alter the hair's surface energy. For example, to improve hair conditioning performance, formulations should modify the surface of the treated hair, making it more hydrophobic, which reduces surface energy.

According to J. Cosmet. Sci., 62, 127-137 (March/April 2011), the surface energy is determined using Fowkes theory, in which the contact angles of the keratin fibers in two solvents (one non-polar and one polar solvent) are first measured and the surface energy is calculated using the Fowkes equation.

In this application, water was used as the polar solvent, and diiodomethane served as the non-polar solvent. In contact angle measurements, diiodomethane is used as the reference liquid for determining the surface energy of solids because it has a relatively high surface tension for a non-polar liquid and therefore forms easily measurable contact angles.

Fowkes theory separates the surface energy into a dispersive component, which is due to the nonpolar interaction at the interface, and a polar component, which arises from the polar interaction at the liquid-solid interface.

Fowkes theory is a combination of three equations that describe the interfacial interactions between a liquid and a solid. Regarding the equations and the method for measuring and calculating surface energy, please refer in full to J. Cosmet. Sci., 62, 127-137 (March/April 2011). The experimental results of this reference demonstrate that reducing or increasing the Hair surface energy can be used to evaluate or screen the performance of cosmetic ingredients and formulations.

Medium (B)

The method according to the invention comprises the application of the agent (B) to the keratin fibers, wherein the agent (B) contains at least one film-forming substance.

Agent (B) preferably contains the film-forming substance(s) in a cosmetic carrier, particularly preferably in a suitable aqueous, alcoholic, or aqueous-alcoholic carrier. Such carriers can be, for example, creams, emulsions, gels, or surfactant-containing foaming solutions, such as shampoos, foam aerosols, foam formulations, or other preparations suitable for application to the hair.

For the purposes of this invention, a film-forming substance is understood to be a monomeric or polymeric organic compound that has good substantivity to the keratin fiber, deposits on its surface, and forms a polymeric film there. Monomeric film-forming substances are reactive and either form the film before or during application in agent (B), or they polymerize directly on the surface of the keratin fiber, thus forming the polymer in situ. Polymeric film formers are, for example, organic polymers with high substantivity to the keratin fiber. High substantivity can be achieved, for example, by the presence of one or more amino groups and/or cationic charges in the polymer backbone.

Particularly suitable film-forming substances are, for example, silanes with one, two or three silicon atoms and film-forming polymers.

In a further particularly preferred embodiment, an agent according to the invention is characterized in that the agent (B) contains at least one film-forming substance selected from the group consisting of silanes having one, two or three silicon atoms and film-forming polymers.

According to the lUPAC rules, the term silane refers to a group of chemical compounds based on a silicon backbone and hydrogen. In organic silanes, the hydrogen atoms are completely or partially replaced by organic groups such as (substituted) alkyl groups and/or alkoxy groups. In organic silanes, some of the hydrogen atoms can also be replaced by hydroxyl groups. Silanes particularly suitable for solving the problem according to the invention are, for example,

- (3-Aminopropyl)triethoxysilane

- (3-Aminopropyl)trimethoxysilane

- (2-Aminoethyl)triethoxysilane

- (2-Aminoethyl)trimethoxysilane

- (3-Dimethylaminopropyl)triethoxysilane

- (3-Dimethylaminopropyl)trimethoxysilane

- (2-Dimethylaminoethyl)triethoxysilane.

und/oder deren Hydrolyse und/oder Kondensationsprodukte. - (2-Dimethylaminoethyl)trimethoxysilane,

and/or their hydrolysis and/or condensation products.

Das vollständige Hydrolyseprodukt von 3-Aminoethyltriethoxysilan und 3-Aminoethyltrimethoxy-silan ist 1-(2-Aminoethyl)silantriol

The complete hydrolysis product of 3-aminopropyltriethoxysilane and 3-aminopropyltrimethoxysilane is 1-(3-aminopropyl)silanetriol

The complete hydrolysis product of 3-aminoethyltriethoxysilane and 3-aminoethyltrimethoxysilane is 1-(2-aminoethyl)silanetriol

Other silanes which are particularly suitable for solving the problem according to the invention are, for example,

- Methyltrimethoxysilane

- Ethyltrimethoxysilane

- Ethyltriethoxysilane

- n-octyltrimethoxysilane

- n-octyltriethoxysilane

- n-dodecyltrimethoxysilane and/or

und/oder deren Hydrolyse und/oder Kondensationsprodukte. - n-Dodecyltriethoxysilane.

and/or their hydrolysis and/or condensation products.

In a further preferred embodiment, a process according to the invention is characterized in that the agent (B) contains as film-forming substance at least one silane selected from the group consisting of (3-aminopropyl)triethoxysilane, (3-aminopropyl)trimethoxysilane, (2-aminoethyl)triethoxysilane, (2-aminoethyl)trimethoxysilane, (3-dimethylaminopropyl)triethoxysilane, (3-dimethylaminopropyl)trimethoxysilane, (2-dimethylaminoethyl)triethoxysilane, (2-dimethylaminoethyl)trimethoxysilane, methyltrimethoxysilane, methyltriethoxysilane,

Ethyltrimethoxysilane, ethyltriethoxysilane, propyltrimethoxysilane, propyltriethoxysilane, hexyltrimethoxysilane, hexyltriethoxysilane, octyltrimethoxysilane, octyltriethoxysilane, dodecyltrimethoxysilane, dodecyltriethoxysilane, octadecyltrimethoxysilane, octadecyltriethoxysilane and/or their hydrolysis and/or condensation products. It has been found to be preferred if the agent (B) - based on the total weight of the agent (B) - contains one or more silanes in a total amount of 0.1 to 20 wt.%, preferably 1 to 15 wt.% and particularly preferably 2 to 12 wt.%.

In addition to the monomeric, reactive substances, polymeric film formers are also very well suited for use in agent (B). It is therefore particularly preferred if at least one film-forming polymer selected from the group consisting of amino-functionalized silicone polymers, chitosan, and cationic polymers, particularly preferably from the group consisting of amino-functionalized silicone polymers and chitosan, is used as the film-forming substance in agent (B).

In a further preferred embodiment, a method according to the invention is characterized in that the agent (B) contains as film-forming substance at least one film-forming polymer selected from the group of amino-functionalized silicone polymers, chitosan and cationic polymers, particularly preferably from the group of amino-functionalized silicone polymers and chitosan.

Silicone polymers are generally macromolecules having a molecular weight of at least 500 g/mol, preferably at least 1000 g/mol, more preferably at least 2500 g/mol, particularly preferably at least 5000 g/mol, which comprise repeating organic units.

The maximum molecular weight of the silicone polymer depends on the degree of polymerization (number of polymerized monomers) and the batch size, and is also determined by the polymerization method. For the purposes of the present invention, it is preferred if the maximum molecular weight of the silicone polymer is not more than 10 ⁷ g/mol, preferably not more than 10 ⁶ g/mol, and particularly preferably not more than 10 ⁵ g/mol.

Silicone polymers comprise many Si-O repeating units, where the Si atoms may carry organic residues such as alkyl or substituted alkyl groups. Alternatively, a silicone polymer is therefore also referred to as polydimethylsiloxane.

In accordance with the high molecular weight of the silicone polymers, these are based on more than 10 Si-O repeating units, preferably more than 50 Si-O repeating units and particularly preferably more than 100 Si-O repeating units, most preferably more than 500 Si-O repeating units.

An amino-functionalized silicone polymer is understood to mean a functionalized silicone which carries at least one structural unit with an amino group. Preferably, the amino-functionalized silicone polymer carries several structural units, each with at least one Amino group. An amino group includes a primary amino group, a secondary amino group, and a tertiary amino group. All of these amino groups can be profaned in an acidic environment and then exist in their cationic form.

In principle, good effects could be achieved with amino-functionalized silicone polymers if they carry at least one primary, at least one secondary and/or at least one tertiary amino group.

In a particularly preferred embodiment, an agent according to the invention

(B) characterized in that it contains at least one amino-functionalized silicone polymer having at least one secondary amino group.

-Amino) The secondary amino group(s) can be located at various positions on the amino-functionalized silicone polymer. Particularly good results were found when using an amino-functionalized silicone polymer that contains at least one, preferably several, structural units of the formula (Si-amino).

-Amino)

In the structural units of the formula (Si-Amino), the abbreviations ALK1 and ALK2 independently represent a linear or branched, divalent Ci-C2o-alkylene group.

-Amino) wobei In a further very particularly preferred embodiment, an agent (B) used in the process according to the invention is characterized in that it contains at least one amino-functionalized silicone polymer which comprises at least one structural unit of the formula (Si-Amino),

-Amino) where

ALK1 and ALK2 independently of each other for a linear or branched, divalent Ci-

C2o-alkylene group.

The positions marked with an asterisk (*) indicate the bond to other structural units of the silicone polymer. For example, the silicon atom adjacent to the star can be bonded to another oxygen atom, and the oxygen atom adjacent to the star can be bonded to another silicon atom or to a C1-C8 alkyl group.

A divalent Ci-C2o-alkylene group can alternatively be referred to as a divalent or divalent Ci-C2o-alkylene group, which means that each group ALK1 or AK2 can form two bonds.

In the case of ALK1, one bond is formed from the silicon atom to the ALK1 group, and the second bond is formed between ALK1 and the secondary amino group.

In the case of ALK2, one bond is formed from the secondary amino group to the ALK2 moiety, and the second bond is formed between ALK2 and the primary amino group.

Examples of a linear divalent C3-C2o-alkylene group include the methylene group (-CH2-), the ethylene group (-CH2-CH2-), the propylene group (-CH2-CH2-CH2-), and the butylene group (-CH2-CH2-CH2-CH2-). The propylene group (-CH2-CH2-CH2-) is particularly preferred. From a chain length of 3 carbon atoms, divalent alkylene groups can also be branched. Examples of branched, divalent C3-C2o-alkylene groups are (-CH2-CH(CH3)-) and (-CH2-CH(CH3)-CH2-). In a further particularly preferred embodiment, the structural units of the formula (Si-Amino) represent repeating units in the amino-functionalized silicone polymer, so that the silicone polymer comprises several structural units of the formula.

(_Si-ll), wobei Particularly stable and uniform films could be obtained when an agent (B) was applied to the keratin fibers in the process, which agent contains at least one amino-functionalized silicone polymer comprising structural units of the formula (Si-I) and the formula (Si-II)

( _Si -ll), where

R1 represents a methyl group or a hydrogen atom, and

R2 represents a Ci-Ce-alkyl group, in particular a methyl group, or a Ci-Ce-alkoxy group, in particular a methoxy group.

In the amino-functionalized silicone polymers (a3), the radical R1 in the structural units of formula (Si-II) represents a methyl group or a hydrogen atom. The radical R2 represents a C1-C8 alkyl group or a C1-C8 alkoxy group. Particularly preferably, the radical R2 represents a methyl group or a methoxy group.

Other particularly suitable film-forming substances from the group of film-forming polymers are chitosan and/or its derivatives.

Chitosan, which can also be referred to as polyglusam or poly-D-glucosamine or polyglucosamine, is a naturally occurring biopolymer derived from chitin, which is composed of ß-1,4-glycosidically linked N-acetylglucosamine residues (precisely 2-acetamido-2-deoxy-ß-D-glucopyranose residues), and is thus, like chitin, a polyaminosaccharide. In the production of chitosan, chitin is deacetylated, so that the molecule ultimately consists only of linearly linked 2-amino-2-deoxy-ß-D-glucopyranose or glucosamine monomers. Chitosan has the CAS number 9012-76-4.

Chitosan is preferably produced from the chitin found in shellfish or crustaceans. Chitosan is industrially obtained from chitin by deacetylation. This can be achieved, for example, using (hot) sodium hydroxide solution or enzymatically. Both processes are used industrially, but the alkaline procedure is clearly the most commonly used. The degree of deacetylation can vary: deacetylation can be complete or partial, resulting in a distribution of highly deacetylated regions alongside less deacetylated regions, or a homogeneous deacetylation distribution. At the same time, this chemical intervention can decrease the chain length of the polymer (depolymerization). The molecular weight of chitosan can vary over a wide range, for example, from 20,000 to approximately 5 million g/mol.

Chitosan derivatives are compounds with a chitosan base structure in which at least some of the functional groups present have been chemically modified. Chitosan derivatives are also based on a poly-D-glucosamine or polyglucosamine structure.

For example, a chitosan with a molecular weight of 20,000 to 800,000 g/mol, preferably 50,000 to 600,000 g/mol, more preferably 80,000 to 450,000 g/mol and most preferably 100,000 to 300,000 g/mol is very suitable.

In a further very particularly preferred embodiment, the agent (B) is characterized in that it contains at least one chitosan and/or a chitosan derivative having a molecular weight of 20,000 to 800,000 g/mol, preferably of 50,000 to 600,000 g/mol, more preferably of 80,000 to 450,000 g/mol and very particularly preferably of 100,000 to 300,000 g/mol.

A chitosan with a molecular weight of 100,000 to 300,000 g/mol can be purchased commercially, for example, from Sigma Aldrich.

A chitosan with a lower molecular weight of 10,000 to 30,000 g/mol (or Dalton) is commercially available in pharmaceutical grade from BioLog Heppe (Kraeber), for example. The degree of deacetylation of this chitosan is 88-95%.

Chitosan in the form of its hydrochloride can be purchased as vegan chitosan from Sandream Impact. The chitosan hydrochloride is a chitosan derivative according to the invention. Chitosan 027 is a suitable, commercially available, high-molecular chitosan from Polymar, which has a molecular weight of 100,000 - 2,000,000 g/mol.

It has proven particularly advantageous if the agent (B) contains the film-forming substance(s) in specific quantity ranges. Particularly good results were obtained when the agent (B) contained one or more film-forming substances in a total amount of 0.1 to 10.0 wt.%, preferably 0.2 to 8.0 wt.%, more preferably 0.5 to 6.0 wt.%, and most preferably 0.7 to 2.5 wt.%, based on the total weight of the agent (B).

Sequence of procedural steps

In principle, the two agents (A) and (B) can be applied to the keratin fibers either simultaneously or sequentially.

If both agents (A) and (B) are used at the same time, this can either mean that the two agents (A) and (B), which were initially provided separately, are mixed together before use to form the ready-to-use agent, or the two agents (A) and (B) are identical, so that agent (A) or (B) contains both the peptide(s) and the film-forming substance(s).

If agents (A) and (B) are applied consecutively, for example, agent (A) can be applied to the keratin fibers first, followed by agent (B). In this embodiment, the peptides are used to prepare or homogenize the keratin surface, and the film-forming agents in agent (B) are applied to the fibers only after the homogenization step. This form of application is particularly preferred.

In principle, it is also possible to first apply agent (B) and then agent (A) to the fibers.

In a further preferred embodiment, a method according to the invention is characterized in that the agents (A) and (B) are applied simultaneously or successively to the keratin fibers.

In principle, the user can freely choose the time period between the application of the two products (A) and (B). However, it may be preferable that no other products, such as other conditioners or styling products, are applied between the application of the two products (A) and (B). For this reason, the maximum time period between the application of the both agents (A) and (B), preferably limited to a time interval of a maximum of 24 hours.

Therefore, a method for treating keratin fibers comprising the following steps in the given order is explicitly preferred:

(1) Application of the agent (A) on the keratin fibers, then

(2) Application of the agent (B) to the keratin fibers, wherein between the application of the agent (A) and the application of the agent (B) there is a period of maximum 24 hours, preferably of maximum 12 hours, more preferably of maximum 6 hours and most preferably of maximum 3 hours.

Also particularly preferred is a method for treating keratin fibers, in particular human hair, comprising the following steps in the order given:

(1) Applying the agent (A) to the keratin fibers,

(2) the agent (A) applied in step (2) is allowed to act on the keratin fibres for a period of 1 to 45 minutes, preferably 5 to 30 minutes,

(3) if necessary, rinsing the agent (A) with water,

(4) if necessary, drying the keratin fibres,

(5) Applying the agent (B) to the keratin fibers, and

(6) Action of the agent (B) on the keratin fibres.

In step (1), the agent (A) is applied to keratin fibers or to the hair. The agent (A) can be applied to dry or water-moistened keratin fibers.

In the next step (2), the previously applied agent (A) is allowed to act on the keratin fibers. Various exposure times from 1 to 45 minutes, preferably from 5 to 30 minutes, are possible.

After the agent (A) has acted on the keratin fibers, it can finally be used in step

(3) rinsed with water, or the agent (A) remains on the keratin fibers and these are dried if necessary.

In step (4), the keratin fibers can be dried if desired. However, it is also possible to apply agent (B) to the still-damp keratin fibers after washing out agent (A). In this embodiment, step (4) is omitted.

In step (5) the agent (B) is then applied to the keratin fibers. The action of the agent (B) on the keratin fibers in step (6) can, for example, take place for a period of 15 seconds to 30 minutes, preferably for a period of 30 seconds to 15 minutes, particularly preferably for a period of 1 to 15 minutes.

Multi-component packaging unit (kit of parts)

To increase user convenience, all necessary resources are preferably provided to the user in the form of a multi-component packaging unit (kit of parts).

A second subject of the present invention is therefore a multi-component packaging unit (kit of parts) for treating keratin fibers, in particular human hair, comprising a first container with agent (A) and a second container with agent (B), which are separately packaged, wherein agents (A) and (B) were disclosed in detail in the description of the first subject of the invention.

Regarding the further preferred embodiments of the multi-component packaging units, what has been said about the method applies mutatis mutandis.

Examples

1. peptides used and their peptide sequences

Table 1

Some of the peptides originate from E. coli display database screenings (e.g., P8C), others are either further developments of these or pure designer peptides (e.g., RAL2QEC and TF12 (RALF-W)).

2. Application of peptides to hair

Hair strands were washed with a 10% aqueous sodium lauryl sulfate solution adjusted to pH 10 with lactic acid, rinsed, and dried.

The hair was then cut into small pieces of 1.5 to 2 cm in length and one portion was placed in an Eppendorf tube. Each peptide was dissolved in water (0.1 mg/ml). A 1.5 ml portion of this solution was added to each portion of cut hair. The Eppendorf tube was sealed and incubated without stirring for one hour at 21 °C.

The supernatant protein solution was then removed as completely as possible with a pipette. The hair was carefully cleaned twice by adding distilled water and then pipetting off the water. The Eppendorf tube was then opened and placed in an oven, and the hair was dried at 37 °C.

The contact angles of the hair treated in this way were measured in water and diiodomethane. The contact angles were measured using the method described in J. Cosmet. Sci. 62, 127-137 (March/April 2011) "Study of hair surface energy and conditioning." The surface free energy was then calculated from the contact angles. The calculation method is disclosed in the same reference. The following values were obtained:

SFE = surface free energy [measured in mJ/mm ² ]

CA = contact angle [measured in degrees °]

DIM = Diiodomethane o = Surface tension

Water

Summary of values:

Compared to untreated hair, the greatest increase in surface energy (SFE, left column) was achieved both at the roots and at the tips by treatment with the peptide Con S5. Therefore, the application of the peptide Con S5 enabled the surface of the hair fiber to be particularly hydrophilized, so that The film-forming substances used adhere particularly well and evenly to the hair fibers.

The use of the peptides PB1, RAL2QEC and G06 also made it possible to increase the surface energy of the hair fibers, particularly in the area of the hair tips, and thus achieve the desired hydrophilization of the surface.

Claims

Patent claims 1. A method for treating keratin fibers, in particular human hair, comprising the following steps: - application of an agent (A) to the keratin fibers, wherein the agent (A) contains at least one peptide comprising or consisting of an amino acid sequence of 5 to 50 amino acids, wherein (Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence, (X _a )nX ₅ X6X7X ₈ X9(Xb)m where each X _a is independently any amino acid, n is an integer from 0 to 45, preferably from 0 to 4, X5 is an amino acid selected from the group consisting of P, H, T, N, R, C and A, Xe is an amino acid selected from the group consisting of T, R, M, G, F, P, N, S, L, Y and W, X7 is an amino acid selected from the group consisting of R, N, S, L, I, Q, W, G, A and Y, Xe is an amino acid selected from the group consisting of K, T, N, A, L, F, D, R and G, X9 is an amino acid selected from the group consisting of R, L, I, A, Q, P, H, G, W and M, each Xb is independently any amino acid, and m is an integer from 0 to 45, preferably from 0 to 7, particularly preferably from 0 to 3, and/or (Ab) the amino acid sequence has at least 85%, preferably at least 86%, more preferably at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with one of the amino acid sequences listed in SEQ ID NOs: 1 - 17, and - application of an agent (B) to the keratin fibers, wherein the agent (B) contains at least one film-forming substance. 2. The method according to claim 1, characterized in that the peptide in the agent (A) (Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence (Xa)nX ₅ X6X7X ₈ X9(Xb)m where X5 is an amino acid selected from the group consisting of P, N, and C, particularly preferably P. 3. Method according to one of claims 1 to 2, characterized in that in the peptide in the agent (A) (Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence (X _a )nX ₅ X6X7X ₈ X9(Xb)m where Xe is an amino acid selected from the group consisting of T, R, M and P, preferably from the group consisting of T, R and M, particularly preferably from the group consisting of T and R. 4. The method according to any one of claims 1 to 3, characterized in that the peptide in the agent (A) (Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence (X _a )nX ₅ X6X7X ₈ X9(Xb)m where X7 is an amino acid selected from the group consisting of R and L, particularly preferably R. 5. The method according to any one of claims 1 to 4, characterized in that the peptide in the agent (A) (Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence (X _a )nX ₅ X6X7X ₈ X ₉ (Xb)m where X ₈ is an amino acid selected from the group consisting of K, T, N and F, preferably from the group consisting of K, T and N, particularly preferably from the group consisting of K and T. 6. The method according to any one of claims 1 to 5, characterized in that the peptide in the agent (A) (Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence (X _a )nX ₅ X6X7X ₈ X ₉ (Xb)m where X9 is an amino acid selected from the group consisting of R, L, A and P, preferably from the group consisting of R, L and P, particularly preferably from the group consisting of R and L, most preferably R. 7. The method according to any one of claims 1 to 6, characterized in that the agent (A) contains at least one peptide which comprises or consists of an amino acid sequence of 7 to 16 amino acids, wherein (Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence (X _a )nX4X ₅ X6X7X ₈ X9Xl0(Xb)m where n stands for the number 0 to 3, preferably for the number 3, X4 is an amino acid selected from the group consisting of R, S, I, V, H, F, T, G, L, E, Q and K, X10 is an amino acid selected from the group consisting of I, K, S, Q, R, L, H, A and F, and m is the number 0 to 6, preferably the number 0 to 2, particularly preferably the number 2. 8. The method according to any one of claims 1 to 7, characterized in that the peptide in the agent (A) (Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence (X _a )nX4X ₅ X6X7X ₈ X9Xl0(Xb)m where X4 is an amino acid selected from the group consisting of R, S, I, F and G, preferably from the group consisting of R, S, I and F, particularly preferably from the group consisting of R, S and I, and/or X10 is an amino acid selected from the group consisting of I, K and R, preferably from the group consisting of I and K, particularly preferably K. 9. The method according to any one of claims 1 to 8, characterized in that the agent (A) contains at least one peptide which comprises or consists of an amino acid sequence of 9 to 16 amino acids, wherein (a) the amino acid sequence in N- to C-terminal orientation has the following sequence (Xa) 0X3X4X5X6X7X3X9X10X11 (Xb)m where n is the number 0 to 2, preferably the number 2, X3 is an amino acid selected from the group consisting of P, R, I, N, C, L, A, V and Q, Xi 1 is an amino acid selected from the group consisting of K, R, I, N, G, E, V, A, S and W, and m is the number 0 to 5, preferably the number 0 or 1, particularly preferably the number 1. 10. The method according to any one of claims 1 to 9, characterized in that the peptide in the agent (A) (Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence (Xa) 0X3X4X5X6X7X8X9X10X11 (Xb)m where X3 is an amino acid selected from the group consisting of P, R and N, preferably from the group consisting of P and R, most preferably R, and/or X11 is an amino acid selected from the group consisting of K and R, most preferably K. 11. The method according to any one of claims 1 to 10, characterized in that the agent (A) contains at least one peptide which comprises or consists of an amino acid sequence of 12 amino acids, wherein (Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence X1X2X3X4X5X6X7X8X9X10X11X12 where Xi is an amino acid selected from the group consisting of Q, R, H, N, I, T, A, D and G, and X2 is an amino acid selected from the group consisting of H, N, M, S, E, W, P, V, A and F, and X12 is an amino acid selected from the group consisting of P, R, Q, I, T, E, N, L, A and G. 12. The method according to any one of claims 1 to 11, characterized in that the peptide in the agent (A) (Aa) the amino acid sequence in N- to C-terminal orientation has the following sequence X1X2X3X4X5X6X7X8X9X10X11X12 where Xi is an amino acid selected from the group consisting of Q, R, I and A, preferably from the group consisting of Q, R and I, particularly preferably Q, and/or X2 is an amino acid selected from the group consisting of H, N, S and P, preferably from the group consisting of H, N and S, particularly preferably N, and/or X12 is an amino acid selected from the group consisting of P, R, Q and T, preferably from the group consisting of P, R and Q, particularly preferably Q. 13. The method according to any one of claims 1 to 12, characterized in that the agent (A) contains at least one peptide which comprises or consists of an amino acid sequence of 5 to 50 amino acids, wherein (Ab) the amino acid sequence has at least 85%, preferably at least 86%, more preferably at least 87%, at least 88%, at least 89%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% or 100% sequence identity with one of the amino acid sequences mentioned in SEQ ID NOs: 1 - 13, preferably with one of the amino acid sequences mentioned in SEQ ID NOs: 1-3, 8 and 13 and very particularly preferably with the amino acid sequence mentioned in SEQ ID NO: 3. 14. The method according to any one of claims 1 to 13, characterized in that the agent (B) contains at least one film-forming substance selected from the group consisting of silanes having one, two or three silicon atoms and film-forming polymers. 15. The method according to any one of claims 1 to 14, characterized in that the agent (B) contains as film-forming substance at least one silane selected from the group consisting of (3-aminopropyl)triethoxysilane, (3-aminopropyl)trimethoxysilane, (2-aminoethyl)triethoxysilane, (2-aminoethyl)trimethoxysilane, (3-dimethylaminopropyl)triethoxysilane, (3-dimethylaminopropyl)trimethoxysilane, (2-dimethylaminoethyl)triethoxysilane, (2-dimethylaminoethyl)trimethoxysilane, methyltrimethoxysilane, methyltriethoxysilane, ethyltrimethoxysilane, ethyltriethoxysilane, propyltrimethoxysilane, propyltriethoxysilane, hexyltrimethoxysilane, hexyltriethoxysilane, octyltrimethoxysilane, octyltriethoxysilane, dodecyltrimethoxysilane, dodecyltriethoxysilane, Octadecyltrimethoxysilane, Octadecyltriethoxysilane and/or their hydrolysis and/or condensation products. 16. The method according to any one of claims 1 to 15, characterized in that the agent (B) contains as film-forming substance at least one film-forming polymer selected from the group consisting of amino-functionalized silicone polymers, chitosan and cationic polymers, particularly preferably from the group consisting of amino-functionalized silicone polymers and chitosan. 17. Method according to one of claims 1 to 16, characterized in that the agents (A) and (B) are applied simultaneously or successively to the keratin fibers. 18. A method according to any one of claims 1 to 17, comprising the following steps in the order given: (1) Application of the agent (A) on the keratin fibers, then (2) Application of the agent (B) to the keratin fibers, wherein between the application of the agent (A) and the application of the agent (B) there is a period of maximum 24 hours, preferably of maximum 12 hours, more preferably of maximum 6 hours and most preferably of maximum 3 hours. 19. Multi-component packaging unit (kit of parts) for treating keratin fibers, in particular human hair, comprising a first container with the agent (A) and a second container with the agent (B) separately packaged, wherein the agents (A) and (B) were defined in claims 1 to 11.