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US20030186854A1 - Antimicrobial peptide, process to obtain a peptide and uses therefor - Google Patents

Antimicrobial peptide, process to obtain a peptide and uses therefor Download PDF

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Publication number
US20030186854A1
US20030186854A1 US10/296,853 US29685303A US2003186854A1 US 20030186854 A1 US20030186854 A1 US 20030186854A1 US 29685303 A US29685303 A US 29685303A US 2003186854 A1 US2003186854 A1 US 2003186854A1
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US
United States
Prior art keywords
arg
cys
peptide
xaa
arachinid
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Abandoned
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US10/296,853
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English (en)
Inventor
Sirlei Daffre
Pedro da Silva
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Universidade de Sao Paulo USP
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Individual
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Assigned to UNIVERSIDADE DE SAO PAULO reassignment UNIVERSIDADE DE SAO PAULO ASSIGNMENT OF ASSIGNORS INTEREST (SEE DOCUMENT FOR DETAILS). Assignors: DA SILVA JR., PEDRO ISMAEL, DAFFRE, SIRLEI
Publication of US20030186854A1 publication Critical patent/US20030186854A1/en
Priority to US11/432,286 priority Critical patent/US7723468B2/en
Abandoned legal-status Critical Current

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    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
    • C07K7/04—Linear peptides containing only normal peptide links
    • C07K7/08—Linear peptides containing only normal peptide links having 12 to 20 amino acids
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P33/00—Antiparasitic agents
    • A61P33/02—Antiprotozoals, e.g. for leishmaniasis, trichomoniasis, toxoplasmosis
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
    • C07K7/64—Cyclic peptides containing only normal peptide links
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
    • Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
    • Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
    • Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change

Definitions

  • the invention refers to small peptides with low hemolytic activity, presenting balanced activity against parasites, fungi and bacteria.
  • protegrins A number of peptides extracted from animals and plants have shown activity against infection.
  • the application PCT WO9503325 published on Feb. 2, 1995, mentions peptides called protegrins, also reviewing literature on this subject, which includes references on tachyplesins, poliphemusins, defensins, ⁇ -defensins and insect defensins.
  • the U.S. Pat. No. 5,994,306 refers to more specific protegrins.
  • This invention has the object to disclose new and small peptides which are similar in some aspects to protegrins, tachytegrins and parevins, but present balanced anti-parasitic, anti-bacteria and anti-fungus activity, besides low hemolitic activity, as well as processes to obtain them and their applications.
  • This is a peptide called gomesin, configured as a clamp-like structure consisting of two anti-parallel beta-folded sheets, joined by a beta turn, containing four invariable cysteine residues forming two disulphide bridges, with the following general formula (1):
  • Z 1 is:
  • X 19 when X 19 is present, a basic, hydrophobic, polar/large or small residue, with a free amino end group available to close the edges of the molecule, such as glutamine or glutamic acid.
  • C 2 , C 6 , C 11 and C 15 are independently cystein, homocystein or pennicilamine;
  • P 1 and P 2 are disulphide bridges from C 2 to C 15 , and from C 6 to C 11 , respectively, either one or both bridges being present;
  • a 3 , A 4 , A 5 , A 12 , A 13 , A 14 , A 16 , A 17 are independently basic, hydrophobic, polar/large or small residues, provided that:
  • a 5 , A 12 and A 14 are preferably hydrophobic residues
  • a 17 is preferably a small residue
  • a 7 to A 10 are residues which are able to effect a beta turn and can be independently basic, hydrophobic, polar/large or small, with at least one of them being basic and the other hydrophobic, with A 8 and A 1 o being preferably basic amino acid residues,
  • a basic, hydrophobic, polar/large or small residue preferably a basic residue, bearing a free carboxyl group or forming an acceptable salt such as potassium, sodium, calcium, magnesium or other with an organic or inorganic ion, or amidated with an amine of the formula NH 3 or RNH 2 or R 2 NH, in which R is independently a saturated or insaturated hydrocarbyl with one to six carbons, such as methyl, ethyl, isopropyl, t-butyl, n-pentyl, cyclohexyl, 2-cyclohexenyl, 3-cyclohexenyl, 4-hexinyl and similar;
  • X 19 when X 19 is present: a basic, hydrophobic, polar/large or small residue, preferably a basic residue, which free carboxyl group end is involved with the closing of peptide molecule edges
  • X 19 may be absent or present; if present, it is a chemical link between Z 1 and A 18 or a chemical structure or molecule present between Z 1 and A 18 is and linked to both, closing the amino acid chain edges of the peptide of the invention;
  • Some of the peptides of the invention can be obtained by extraction from animals, such as from the spider Acanthoscurria gomesiana , and due to this origin they are called gomesins. They can also be synthetically produced and, when containing only genetically coded amino acids, they can be produced in a recombinant way. Peptides of the invention are useful for the treatment and prevention of animal and plant infection as caused by parasites, bacteria and/or fungi. In another aspect, DNA coding peptides of the invention may be expressed in situ, in animals or plants, to fight infection. Peptides of the invention can also be used as standard for antimicrobial tests and for binding to endotoxins.
  • Peptides of the invention can be obtained in a recombinant way by means of peptide-coding cDNA expression in heterologous systems, as well known in the literature.
  • the invention also refers to useful compositions against bacteria, fungi and parasites, used in the combat against such organisms.
  • Peptides of the invention are generally different from others known in the art, among other reasons, for presenting the following qualities which had not been simultaneously found so far:
  • dissulphide bridges can be substituted by lactam bridges or any other bridge playing an equivalent role.
  • amino and carboxy ends may be derived.
  • the amino group end may be methyled, carbamyled, acyled, acetylated or as pyroglutamic acid.
  • Peptides of the invention may, by means of addition to the carboxyl end of the molecules, be present as inorganic salts, such as chloride, bromide, iodide, fluoride, sulphate, nitrate, phosphate, etc., or organic salts, such as acetate, formate, benzoate, etc. The acceptance of each one of the above salts depends on the desired use, which is routinely understood.
  • the carboxyl end can also be amidated. Derivation reactions are known.
  • amino acid residues of the peptides of the invention are defined under the following characteristics:
  • the residue has a positive charge due to its association with the H ion under physiologic pH, and the residue is attracted to an acquous solution, so to seek superficial positions in the configuration of a peptide in which it is contained, provided that it is in acquous media with physiologic pH;
  • hydrophobic the residue is not charged under physiologic pH and is repelled by an acquous solution, so to seek more internal positions in the configuration of a peptide in which it is contained, provided that the peptide is in acquous media;
  • polar/small neutral residue, since its side chains are not sufficiently large, even if polar groups are absent, to make them become hydrophobic. It contains four or less carbons when at least one polar group appears in the side chain and three or less carbons when this is not the case.
  • acids aspartic acid, glutamic acid
  • non cyclic arginine, lysine
  • hydrophobic tyrosine, valine, isoleucine, leucine, methyonine, phenyl alanine, tryptophan.
  • the functional equivalents of the peptide of the invention are also the said compounds where one or several aminoacids are enantiomers, diastereoisomers, natural aminoacids with a D-conformation, unusual aminoacids such as Ca—methyl—aminoacid, hydroxylysine, methyllysine, dimethyllysine and preferentially pyroglutamic acid at the particular position of the residue A1 at the N-terminus of the said compounds.
  • the invention is also covering the retropeptides and the retro-inversopeptides and the synthetic aminoacids such as the ornithine, the norleucine, the cyclohexyl-alanine and omega-aminoacids.
  • Z 1 is pyroglutamic acid
  • a 3 , A 4 , A 8 , A 10 and A 16 are basic residues, with preferably A 3 , A 4 , A 10 and A 16 being arginine and A 8 being lysine;
  • a 18 is a basic residue, preferably amidated arginine, optionally non-amidated;
  • a 5 , A 7 , A 12 and A 14 are hydrophobic residues, with preferably A 5 being leucine, A 7 and A 14 being tyrosine and A 12 being valine;
  • a 9 is a polar/large residue, preferably glutamine
  • a 13 and A 17 are small residues, preferably with A 13 being threonine and A 17 being glycine.
  • Z 1 is a basic amino acid, hydrophobic, polar/large or small residue with a free amino group end, e.g. glutamine.
  • a 18 is a basic residue, with a free carboxyl end group involved in closing peptide edges.
  • X 19 is a chemical structure present between Z 1 and A 18 , connected to both so to close the peptide chain edges.
  • R a arginine with an amidated carboxyl group end
  • Hemolymph (approximately 0.4 ml/spider) of both male and female animals in different development stages was collected from pre-cooled animals by heart puncture with an apyrogenic syringe, in the presence of sodium citrate buffer (30 mmol/L, pH 4.6) containing NaCl (450 mmol/L), EDTA (10 mmol/L) and glucose (100 mmol/L). Hemocytes are removed from plasma by centrifugation at 800 ⁇ g for 10 minutes at 4° C. Entire hemocytes are washed once with sodium citrate buffer and lysated by concentration in a vacuum centrifuging machine.
  • hemocytes are re-suspended in a 1.5 ml of 2M acetic acid supplemented with aprotinin (20 ⁇ g/ml) as protease inhibitor, being homogenized in a Dounce equipment (maximum 152 ⁇ , minimum 76 ⁇ ).
  • a second homogenization is effected by means of sonication (3 ⁇ 30s) at average intensity, kept in an ice cold water bath and the extraction is effected for 30 minutes at 4° C. under mild stiring.
  • the supernatant obtained by means of centrifugation at 13,800 ⁇ g for 30 minutes at 6° C. is directly submitted to pre-purification by solid phase extraction.
  • Organella and cytosolic acid extracts are applied to solid phase columns connected in series, balanced in acidic water (0.05% trifluoroacetic acid). Three elutions are successively effected with 5%, 40% and 80% acetonitrile in acidic water. The 40% acetonitrile portion is concentrated by centrifugation under vacuum, reconsistuted with MiliQ water and reverse phase chromatographed in a column which is balanced with 2% acetonitrile in acidified water. Elution was performed with a linear gradient of acetonitrile from 2 to 60% in acidified water for 120 minutes, at a flow rate of 1.3 ml/min.
  • the active fraction against the tested bacterium Micrococcus luteus of hemocytes is additionally purified by filtration chromatography. Elution is made under isocratic conditions with 30% acetonitrile in acidic water at a flow rate of 0.4 ml/min.
  • HPLC high pressure liquid chromatography
  • Peptides of the invention have been synthesized using a classic Fmoc procedure as described in J. Biol. Chem., 271, 29537-29544 (1996).
  • FIG. 1 attached shows a table regarding the activity spectrum for gomesin, both amidated (Example 1)and non-amidated (Example 2), against bacteria, fungi and yeast.
  • the evaluation of activity against bacteria and fungi was done as described in J. Biol. Chem., 271, 29537-29544 (1996).
  • n. d. means “non-detected” for the tested concentration range of up to 100 ⁇ M for gomesin and 50 ⁇ M for androctonin, while n. m. means not measured.
  • the table shows that the peptides of the invention have anti-bacteria properties.
  • gomesin from Example 1 above
  • MIC minimum inhibitory concentration
  • Anti-bacterial properties have also been verified in the peptides of the invention, e.g. by the mortality of Micrococcus luteus and Entamoeba coli D22 as shown in FIG. 2.
  • 10 ⁇ M of the gomesin of Example 1 (solid line) or water (dotted line) have been added to an exponential stage culture of M. luteus (circles) or E.
  • Antibodies to the peptides of the invention can be produced by making use of standard immunologic technics for the production of policlonal antibodies and, if required, by perpetuating antibody producing cells of the immunized host as a source for the production of monoclonal antibodies.
  • Peptides of the invention may be used in various compositions which are active against bacteria, fungi and parasites. They can be used individually, as a mixture with other peptides of the invention, with other microbicidal agents or both, and jointly with other ingredients known in the art, e.g. active principles such as erythromicine, tetracycline, azithromicine, cephalosporines, etc. and general constituents such as carriers, diluents, excipients, etc.
  • active principles such as erythromicine, tetracycline, azithromicine, cephalosporines, etc.
  • general constituents such as carriers, diluents, excipients, etc.
  • Peptides of the invention may be formulated for pharmaceutical or veterinary use.
  • formulations of the invention can be presented in any form, adapted to the intended purpose as well known by an expert in the art, e.g. for topic use such as creams, oils, ointments, powders, gels, etc. or appropriately for oral, transdermal, transmucous, intramuscular, intravenous, subcutaneous, etc. administration.

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  • Chemical & Material Sciences (AREA)
  • Organic Chemistry (AREA)
  • Health & Medical Sciences (AREA)
  • General Health & Medical Sciences (AREA)
  • Medicinal Chemistry (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Biophysics (AREA)
  • Biochemistry (AREA)
  • Genetics & Genomics (AREA)
  • Molecular Biology (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Veterinary Medicine (AREA)
  • Tropical Medicine & Parasitology (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • General Chemical & Material Sciences (AREA)
  • Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
  • Pharmacology & Pharmacy (AREA)
  • Animal Behavior & Ethology (AREA)
  • Public Health (AREA)
  • Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
  • Peptides Or Proteins (AREA)
US10/296,853 2000-05-29 2001-05-29 Antimicrobial peptide, process to obtain a peptide and uses therefor Abandoned US20030186854A1 (en)

Priority Applications (1)

Application Number Priority Date Filing Date Title
US11/432,286 US7723468B2 (en) 2000-05-29 2006-05-10 Antimicrobial peptide, compositions, and uses therefor

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
BRPI0001870-8A BR0001870B1 (pt) 2000-05-29 2000-05-29 Peptídeo, processo de obtenção de peptídeo, formulação compreendendo peptídeo, método de prevenção de crescimento de parasitas, fungos e bactérias, método para inativar a endotoxina de bactérias gram-negativas
BRPI0001870-8 2000-05-29

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US11/432,286 Continuation-In-Part US7723468B2 (en) 2000-05-29 2006-05-10 Antimicrobial peptide, compositions, and uses therefor

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AU (1) AU6367601A (fr)
BR (1) BR0001870B1 (fr)
WO (1) WO2001092290A2 (fr)

Cited By (2)

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US20060094082A1 (en) * 2004-10-26 2006-05-04 Agennix Incorporated Composition of lactoferrin related peptides and uses thereof
US11174288B2 (en) 2016-12-06 2021-11-16 Northeastern University Heparin-binding cationic peptide self-assembling peptide amphiphiles useful against drug-resistant bacteria

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HK1208039A1 (en) 2011-12-29 2016-02-19 Dana-Farber Cancer Institute, Inc. Stabilized antiviral fusion helices
WO2014144768A2 (fr) 2013-03-15 2014-09-18 Dana-Farber Cancer Institute, Inc. Peptides bh4 stabilisés et leurs utilisations
CA2906572A1 (fr) 2013-03-15 2014-09-25 Dana-Farber Cancer Institute, Inc. Peptide d'ezh2 stabilise
US10087215B2 (en) 2013-03-15 2018-10-02 Dana-Farber Cancer Institute, Inc. Stabilized SOS1 peptides
JP2018511594A (ja) 2015-03-18 2018-04-26 マサチューセッツ インスティテュート オブ テクノロジー 選択的ｍｃｌ−１結合ペプチド
WO2017004591A2 (fr) 2015-07-02 2017-01-05 Dana-Farber Cancer Institute, Inc. Peptides stabilisés anti-microbiens
CA2995479A1 (fr) 2015-08-28 2017-03-09 Dana-Farber Cancer Institute, Inc. Peptides se liant a bfl -1
JP7105696B2 (ja) 2016-02-29 2022-07-25 デイナ ファーバー キャンサー インスティチュート，インコーポレイテッド 感染症を治療するステープル化細胞内ターゲティング抗微生物ペプチド
US11198715B2 (en) 2016-07-22 2021-12-14 Massachusetts Institute Of Technology Selective Bfl-1 peptides
JP7069126B2 (ja) 2016-08-26 2022-05-17 デイナ ファーバー キャンサー インスティチュート，インコーポレイテッド 化学療法誘発性末梢性ニューロパシーおよび難聴を処置または予防するためのｂｃｌ－ｗポリペプチドおよび模倣物
EP3551213A4 (fr) 2016-12-07 2020-11-04 The University of Chicago Compositions et procédés d'inhibition de fox3
AU2018304230A1 (en) 2017-07-19 2020-02-06 Dana-Farber Cancer Institute, Inc. Stabilized anti-microbial peptides for the treatment of antibiotic-resistant bacterial infections
WO2019090267A1 (fr) * 2017-11-03 2019-05-09 The Regents Of The University Of California Procédés et compositions utiles pour inhiber la croissance de certaines bactéries
CA3079758A1 (fr) 2017-12-15 2019-06-20 Dana-Farber Cancer Institute, Inc. Ciblage selectif des proteines d'apoptose par des peptides noxa structuralement stabilises et/ou reactifs a la cysteine
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US11952432B2 (en) 2018-02-07 2024-04-09 Dana-Farber Cancer Institute, Inc. Cell-permeable stapled peptide modules for cellular delivery
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EP4077361A1 (fr) 2019-12-16 2022-10-26 Dana-Farber Cancer Institute, Inc. Peptides oncolytiques structurellement stabilisés et leurs utilisations
WO2021127493A1 (fr) 2019-12-20 2021-06-24 Dana-Farber Cancer Institute, Inc. Peptides type peptide 1 apparenté au glucagon structuralement stabilisés et leurs utilisations
KR20220148869A (ko) 2020-03-04 2022-11-07 다나-파버 캔서 인스티튜트 인크. 구조적으로 안정화된 항바이러스성 SARS-CoV-2 펩타이드 및 그의 용도
WO2021216845A1 (fr) 2020-04-22 2021-10-28 Dana-Farber Cancer Institute, Inc. Peptides de type hélice 1 d'ace2 antiviraux structuralement stabilisés et leurs utilisations
WO2021222243A2 (fr) 2020-04-27 2021-11-04 Dana-Farber Cancer Institute, Inc. Peptides p53 structuralement stabilisés et sélectifs de hdmx et leurs utilisations
JP2023546561A (ja) 2020-10-14 2023-11-06 デイナ ファーバー キャンサー インスティチュート，インコーポレイテッド ウイルスタンパク質および宿主タンパク質の分解のためのキメラコンジュゲートならびに使用方法
EP4240395A1 (fr) 2020-11-05 2023-09-13 Dana-Farber Cancer Institute, Inc. Peptides antiviraux structurellement stabilisés pour lutter contre le virus ebola et leurs utilisations
IL311151A (en) 2021-09-08 2024-04-01 Dana Farber Cancer Inst Inc Structurally clamped antiviral SARS-COV-2 peptide-cholesterol conjugates and uses thereof
US20250288658A1 (en) 2022-05-04 2025-09-18 Dana-Farber Cancer Institute, Inc. Ebolavirus surface glycoprotein peptides, conjugates, and uses thereof
EP4532513A1 (fr) * 2022-05-27 2025-04-09 Fundación Privada Instituto De Salud Global Barcelona Peptides cycliques ayant une activité antibactérienne dirigée contre des pathogènes multirésistants aux médicaments (mdr)

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US5994306A (en) * 1995-11-22 1999-11-30 Intrabiotics Pharmaceuticals, Inc. Fine-tuned protegrins

Patent Citations (1)

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Cited By (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US20060094082A1 (en) * 2004-10-26 2006-05-04 Agennix Incorporated Composition of lactoferrin related peptides and uses thereof
US7183381B2 (en) 2004-10-26 2007-02-27 Agennix, Inc. Composition of lactoferrin related peptides and uses thereof
US20070142292A1 (en) * 2004-10-26 2007-06-21 Agennix Incorporated Composition of lactoferrin related peptides and uses thereof
US7420033B2 (en) 2004-10-26 2008-09-02 Agennix, Inc. Composition of lactoferrin related peptides and uses thereof
US11174288B2 (en) 2016-12-06 2021-11-16 Northeastern University Heparin-binding cationic peptide self-assembling peptide amphiphiles useful against drug-resistant bacteria
US12319752B2 (en) 2016-12-06 2025-06-03 Northeastern University Heparin-binding cationic peptide self-assembling peptide amphiphiles useful against drug-resistant bacteria

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US20060276380A1 (en) 2006-12-07
BR0001870B1 (pt) 2014-02-25
AU6367601A (en) 2001-12-11
BR0001870A (pt) 2002-01-02
WO2001092290A3 (fr) 2002-08-15
WO2001092290A2 (fr) 2001-12-06
US7723468B2 (en) 2010-05-25

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Effective date: 20030224

STCB Information on status: application discontinuation

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