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WO2024181766A1 - Composite, composition pour analyse de turbidité comprenant celui-ci, et son procédé de fabrication - Google Patents

Composite, composition pour analyse de turbidité comprenant celui-ci, et son procédé de fabrication Download PDF

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Publication number
WO2024181766A1
WO2024181766A1 PCT/KR2024/002500 KR2024002500W WO2024181766A1 WO 2024181766 A1 WO2024181766 A1 WO 2024181766A1 KR 2024002500 W KR2024002500 W KR 2024002500W WO 2024181766 A1 WO2024181766 A1 WO 2024181766A1
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complex
beads
protein
blocking agent
producing
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Korean (ko)
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신재호
이정봉
이두현
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I Corebio Inc
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I Corebio Inc
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    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
    • G01N33/531—Production of immunochemical test materials

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  • Various embodiments of the present invention relate to a complex, a composition for turbidity analysis comprising the same, and a method for preparing the same. More specifically, the present invention relates to a complex for turbidity analysis having improved accuracy and sensitivity, a composition for turbidity analysis comprising the same, and a method for preparing the same.
  • the most ideal method in modern disease diagnosis methods is a diagnostic method that is fast, accurate, and has a simple procedure.
  • various diseases are diagnosed using biological samples (blood, urine, etc.), and various measurement methods are developed and used as such diagnostic methods.
  • Representative methods of such measurement methods include biochemical measurement methods using enzyme reactions or immunoassay methods using antigen-antibody reactions.
  • a method of diagnosing diseases through turbidity analysis caused by aggregation by antigen-antibody binding has also been widely used.
  • a complex according to various embodiments of the present invention comprises a bead; a blocking agent coating the bead; and a protein chemically cross-linked with the blocking agent.
  • composition for turbidity analysis according to various embodiments of the present invention comprises the complex.
  • a method for manufacturing a complex comprises the steps of preparing beads; coating the beads with a blocking agent; and chemically cross-linking the blocking agent and a protein.
  • the complex according to various embodiments of the present invention has excellent structural stability and can increase accuracy in turbidity analysis by including a bead coated with a blocking agent and a protein (antigen or antibody) chemically cross-linked with the blocking agent.
  • Figure 1 is a schematic diagram of a complex according to various embodiments of the present invention.
  • FIG. 2 is a schematic diagram illustrating a method for manufacturing a complex according to various embodiments of the present invention.
  • Figure 3 is a schematic diagram explaining the influence according to antigen size.
  • Figure 4 is a graph comparing the performance of the ASO detection sensor according to Experimental Example 1-1.
  • Figure 5 shows the results of the precision evaluation according to Experimental Example 1-2.
  • Figure 6 shows the results of the accuracy evaluation according to Experimental Example 1-3.
  • Figure 7 shows the results of stability evaluation according to Experimental Example 1-4.
  • Figure 8 shows the results of the ASO detection evaluation in whole blood according to Experimental Example 1-5.
  • Figure 9 is a graph comparing the performance of the TP detection sensor according to Experimental Example 2-1.
  • Figure 10 shows the results of precision evaluation according to Experimental Example 2-2.
  • Figure 11 shows the results of the accuracy evaluation according to Experimental Example 2-3.
  • Figure 12 shows the results of stability evaluation according to Experimental Example 2-4.
  • Figure 13 shows the results of the evaluation of TP detection in whole blood according to Experimental Example 2-5.
  • Figure 14 is a graph comparing the performance of the C-peptide detection sensor according to Experimental Example 3-1.
  • Figure 15 shows the results of the precision evaluation according to Experimental Example 3-2.
  • Figure 16 shows the results of accuracy evaluation according to Experimental Example 3-3.
  • Figure 17 shows the results of stability evaluation according to Experimental Example 3-4.
  • Figure 18 shows the results of the evaluation of C-peptide detection in whole blood according to Experimental Example 3-5.
  • a complex (10) may include a bead (100), a blocking agent (200), and a protein (400).
  • the bead (100) may be at least one selected from the group consisting of latex beads, polymer plastic beads, polystyrene beads, beads made of biocompatible polymers, glass beads, and silica beads.
  • the bead (100) may be a latex bead.
  • the diameter of the bead (100) of the present invention may be 100 nm or less.
  • a complex (10) having excellent stability and also excellent sensitivity in turbidity analysis can be provided.
  • the blocking agent (200) can coat the bead (100).
  • the blocking agent (200) can uniformly coat the surface of the bead (100).
  • the blocking agent (200) can be at least one selected from the group consisting of albumin, casein, skim milk, gelatin, and serum.
  • the blocking agent (200) of the present invention may not have undergone additional modification. Therefore, it is possible to prevent side reactions that may occur during additional modification of the blocking agent or formation of disulfide bonds during the reaction.
  • the protein (400) can be chemically cross-linked with the blocking agent (200).
  • the protein (400) can be chemically cross-linked with the blocking agent (200) via a linker (300).
  • linker 300 by using a specific type of linker (300), it is possible to prevent modification of the protein (400), particularly modification of the active site (410), and maintain a high activity of specific binding.
  • a specific type of linker such as 1,6-hexanediol diglycidyl ether, accuracy, precision, stability, etc. may be excellent during turbidity analysis.
  • the protein (400) may be an antigen or antibody (fragment antibody) that can recognize a specific protein and form a specific binding.
  • the protein (400) is characterized by having a size of 100 kDa or less. That is, in the present invention, a complex capable of turbidity analysis can be provided using a protein of very small size.
  • the protein (400) includes an active site (410). That is, the protein (400) includes a portion capable of forming a specific bond with a specific protein. At this time, in the present invention, the protein (400) may have a terminal crosslinkable with the blocking agent (200) positioned at the inactive site (420). Therefore, the inactive site (420) of the protein (400) may be crosslinked with the blocking agent (200). That is, in the present invention, the active site (410) of the protein (400) is not crosslinked with the blocking agent (200). Through this, the active site (410) of the protein (400) may not be covered by the blocking agent (200).
  • the complex (10) according to various embodiments of the present invention has excellent structural stability and can increase accuracy in turbidity analysis by including a bead (100) coated with a blocking agent (200) and a protein (400) chemically cross-linked with the blocking agent (200).
  • the protein (400) when bound to the blocking agent (200), there is no three-dimensional structural deformation of the complex (10), and the protein (400) in the complex (10) can maintain the active site (410) without a portion being covered by the blocking agent (200), thereby improving sensitivity.
  • composition for turbidity analysis of the present invention may include the complex described above.
  • the composition for turbidity analysis of the present invention may improve accuracy and sensitivity during turbidity analysis by including the complex described above.
  • a method for manufacturing a complex of the present invention may include a step of preparing beads; a step of coating the beads with a blocking agent; and a step of chemically cross-linking the blocking agent and the protein.
  • a bead (100) at least one selected from the group consisting of latex beads, polymer plastic beads, polystyrene beads, beads made of a biocompatible polymer, glass beads, and silica beads can be prepared.
  • the bead (100) and the blocking agent (200) can be mixed and reacted under constant temperature and humidity conditions.
  • the blocking agent (200) can be at least one selected from the group consisting of albumin, casein, skim milk, gelatin, and serum.
  • Beads (100) coated with a blocking agent (200) can be centrifuged, washed, and dispersed.
  • additional modification steps such as introduction of a functional group or substitution of a functional group into the bead (100) and/or the blocking agent (200) are omitted. That is, in the present invention, a bead (100) coated with a blocking agent (200) can be manufactured without an additional modification step.
  • the step of chemically crosslinking the blocking agent (200) and the protein (400) may include a step of activating the functional group of the blocking agent (200). That is, the blocking agent (200) and the protein (400) may be chemically crosslinked after the functional group of the blocking agent (200) is activated.
  • the step of chemically crosslinking the blocking agent (200) and the protein (400) may include a step of activating the functional group of the protein (400). That is, the blocking agent (200) and the protein (400) may be chemically crosslinked after the functional group of the protein (400) is activated.
  • linker (300) selected from the group consisting of (1-ethyl-3-(-3-dimethylaminopropyl) carbodiimide, N', N'-dicyclohexyl carbodiimide, 4-(4,6-dimethoxy-1,3,5-triazin-2-yl)-4-methylmorpholinium chloride, Glutaraldehyde, Poly(ethylene glycol
  • a linker (300) can be added to a bead (100) coated with a blocking agent (200) and reacted. Afterwards, centrifugation, washing, and dispersion processes can be performed.
  • the pH when adding a linker (300), the pH can be adjusted to 7 to 8. Through this, the activity for chemical crosslinking of the blocking agent (200) and the protein (400) can be promoted, and crosslinking can be achieved without a three-dimensional structural change of the complex (10).
  • Example 1-1 Synthesis of the complex of the present invention
  • casein As a blocking agent, 4 mL of casein (PBS, 1%) and 1 mL of the previously prepared solution were added, and the mixture was stirred for 15 hours using a rotator. Next, casein-latex particles were separated by centrifugation. After that, washing was repeated twice. At this time, washing can be performed through the following process. After removing the supernatant, 5 mL of 25 mM phosphate (pH 7.4) is added, excluding only the pellet, which is a lump of settled particles at the bottom. Next, dispersion is performed for about 1 minute using a tip sonicator, and centrifugation is performed.
  • casein As a blocking agent, 4 mL of casein (PBS, 1%) and 1 mL of the previously prepared solution were added, and the mixture was stirred for 15 hours using a rotator. Next, casein-latex particles were separated by centrifugation. After that, washing was repeated twice. At this time, washing can be performed through the following process. After removing the supernatant, excluding only the pellet, which is a lump of settled particles at the bottom, 5 mL of 25 mM phosphate (pH 7.4) is added. Next, dispersion is performed for about 1 minute using a tip sonicator, and centrifugation is performed.
  • a complex was prepared by first cross-linking the protein to the beads and then blocking with a blocking agent.
  • the specific manufacturing method is as follows.
  • Streptolysin O Antigen (192 ⁇ L) was added as a protein and left at room temperature for 1 hour to adjust the pH to 7 to 8. Next, the mixture was stirred on a rotator for 15 hours. Afterwards, centrifugation was performed.
  • the protein was first cross-linked to the beads and then blocked with a blocking agent, and it was confirmed that the accuracy of turbidity analysis was reduced because the active site of the protein was covered by the blocking agent or there was no directionality upon substitution.
  • the blocking agent due to the low stability of the physically adsorbed protein, it may fall off from the beads during blocking, and there is a possibility that non-specific binding may occur due to the fallen protein.
  • the complex 37.5 ⁇ L according to Example 1-2 and the sample dilution solution 580.5 ⁇ L were mixed. Then, 618 ⁇ L of the mixed solution was injected into the cuvette. The cuvette and the body were combined to prepare a cartridge. Antibody calibrators were prepared at 0, 125, 250, 500, and 1000 IU/mL, and 5 ⁇ L of ASO antibody was injected into the tip. Then, after combining the cartridge to the equipment, the Optical Density was measured, and the calibrator of the same concentration was measured three times.
  • the standard deviation of the measurement values was all 0.004 or less, and the coefficient of variation (CV) was also very low, within 5%. That is, it can be seen that the complex according to Example 1-2 has excellent precision and reproducibility in turbidity analysis.
  • Antibody concentration Average of measurements Standard deviation of measurements %CV 125 0.0229 0.0010 4.3 250 0.0497 0.0006 1.2 500 0.1050 0.0021 2.0 1,000 0.1659 0.0039 2.4
  • the complex 37.5 ⁇ L and the sample dilution 580.5 ⁇ L according to Example 1-2 were mixed. Then, 618 ⁇ L of the mixed solution was injected into the cuvette. The cuvette and the body were combined to prepare a cartridge. Antibody calibrator 0, 500 IU/mL and Positive control 280, 430 IU/mL were prepared, and 5 ⁇ L of antibody or 5 ⁇ L of Positive control was injected into the tip. After that, the cartridge was combined with the equipment and the Optical Density was measured.
  • the measured values in the positive control were approximately 0.0861 and 0.1248, respectively, and the antibody concentrations calculated through the calibrator were confirmed to be almost similar at 284 to 289 and 406 to 419 IU/mL, respectively. That is, it can be seen that the complex according to Example 1-2 has excellent accuracy in turbidity analysis.
  • Example 1-2 The complex according to Example 1-2 (37.5 ⁇ L) and the sample dilution (580.5 ⁇ L) were mixed. Then, 618 ⁇ L of the mixed solution was injected into the cuvette. The cuvette and the body were combined to prepare a cartridge. Antibody calibrators were prepared at 0, 125, 250, 500, and 1000 IU/mL, and 5 ⁇ L of ASO antibody was injected into the tip. Then, the cartridge was combined with the equipment, and the Optical Density was measured over time (0, 2, 5, 7, 14, 21, and 28 days).
  • the measured values in the whole blood sample were approximately 0.0624 and 0.0937, respectively, and the antibody concentrations calculated through the calibrator were confirmed to be almost similar at 227 to 234 and 341 to 352 IU/mL, respectively. That is, it can be seen that the complex according to Example 1-2 has excellent accuracy in turbidity analysis.
  • casein As a blocking agent, 4 mL of casein (PBS, 1%) and 1 mL of the previously prepared solution were added, and the mixture was stirred for 15 hours using a rotator. Next, casein-latex particles were separated by centrifugation. After that, washing was repeated twice. At this time, washing can be performed through the following process. After removing the supernatant, 5 mL of 25 mM phosphate (pH 7.4) is added, excluding only the pellet, which is a lump of settled particles at the bottom. Next, dispersion is performed for about 1 minute using a tip sonicator, and centrifugation is performed.
  • Treponema pallidum Antigen with a size of 47 kDa as a protein was added and stirred for 2 hours using a rotator. Afterwards, centrifugation was performed and washing was repeated twice. At this time, washing can be performed through the following process. After removing the supernatant except for the pellet, 4 mL of 25 mM phosphate buffer (pH 7.4) is added. Next, dispersion is performed using Tip sonication and centrifugation is performed.
  • casein As a blocking agent, 4 mL of casein (PBS, 1%) and 1 mL of the previously prepared solution were added, and the mixture was stirred for 15 hours using a rotator. Next, casein-latex particles were separated by centrifugation. After that, washing was repeated twice. At this time, washing can be performed through the following process. After removing the supernatant, 5 mL of 25 mM phosphate (pH 7.4) is added, excluding only the pellet, which is a lump of settled particles at the bottom. Next, dispersion is performed for about 1 minute using a tip sonicator, and centrifugation is performed.
  • a complex was prepared by first cross-linking the protein to the beads and then blocking with a blocking agent.
  • the specific manufacturing method is as follows.
  • Treponema pallidum antigen 158 ⁇ L of Treponema pallidum antigen was added as a protein and left at room temperature for 1 hour to adjust the pH to 7 to 8. Next, it was stirred on a rotator for 15 hours. Afterwards, centrifugation was performed.
  • Example 2-1 Using the complexes according to Example 2-1, Example 2-2 and Comparative Example 2-1, the same evaluation method as in Experimental Example 1-1 was used for evaluation, but 70 ⁇ L of the complex and 490 ⁇ L of the sample dilution solution were mixed, and 10 ⁇ L of TP antibody was injected instead of ASO antibody for the experiment.
  • TP antibody used was 0, 18, 39, 121 and 256 T.U.
  • the protein was first cross-linked to the beads and then blocked with a blocking agent, and it was confirmed that the accuracy of turbidity analysis was reduced because the active site of the protein was covered by the blocking agent or there was no directionality upon substitution.
  • the blocking agent due to the low stability of the physically adsorbed protein, it may fall off from the beads during blocking, and there is a possibility that non-specific binding may occur due to the fallen protein.
  • Example 2-2 The complex according to Example 2-2 was evaluated using the same evaluation method as in Experimental Example 1-2, but 70 ⁇ L of the complex and 490 ⁇ L of the sample dilution solution were mixed, and 10 ⁇ L of TP antibody was injected instead of ASO antibody for the experiment.
  • TP antibody used was 0, 18, 39, 121, and 256 T.U.
  • the standard deviation of the measurement values was all less than 0.006, and the coefficient of variation (CV) was also very low at less than 4%. That is, it can be seen that the complex according to Example 2-2 has excellent precision and reproducibility in turbidity analysis.
  • Antibody concentration Average of measurements Standard deviation of measurements %CV 18 0.0334 0.0013 3.8 39 0.06151 0.0012 2.0 121 0.1271 0.0031 2.4 256 0.1900 0.0055 2.9
  • Example 2-2 The complex according to Example 2-2 was evaluated using the same evaluation method as in Experimental Example 1-3, but 70 ⁇ L of the complex and 490 ⁇ L of the sample dilution solution were mixed, and 10 ⁇ L of TP antibody was injected instead of ASO antibody for the experiment. TP antibody 0, 256 T.U and positive control 100, 170 T.U were used.
  • the measured values in the positive control were approximately 0.0689 and 0.1190, respectively, and the antibody concentrations calculated through the calibrator were confirmed to be almost similar at 89 to 97 and 156 to 167 T.U., respectively. That is, it can be seen that the complex according to Example 2-2 has excellent accuracy in turbidity analysis.
  • Example 2-2 The complex according to Example 2-2 was evaluated using the same evaluation method as in Experimental Example 1-4, but 70 ⁇ L of the complex and 490 ⁇ L of the sample dilution solution were mixed, and 10 ⁇ L of TP antibody was injected instead of ASO antibody for the experiment.
  • TP antibody used was 0, 18, 39, 121, and 256 T.U.
  • Example 2-2 The complex according to Example 2-2 was evaluated using the same evaluation method as in Experimental Example 1-5, but 70 ⁇ L of the complex and 490 ⁇ L of the sample dilution solution were mixed, and 10 ⁇ L of TP antibody and 20 ⁇ L of whole blood sample were injected instead of ASO antibody for the experiment. 0, 256 T.U of TP antibody and 89, 154 T.U of whole blood sample were used.
  • the measurement values measured in the whole blood sample were approximately 0.0621 and 0.1059, respectively, and the antibody concentrations calculated through the calibrator were confirmed to be almost similar at 80 to 88 and 138 to 150 T.U., respectively. That is, it can be seen that the complex according to Example 2-2 has excellent accuracy in turbidity analysis.
  • casein As a blocking agent, 4 mL of casein (PBS, 1%) and 1 mL of the previously prepared solution were added, and the mixture was stirred for 15 hours using a rotator. Next, casein-latex particles were separated by centrifugation. After that, washing was repeated twice. At this time, washing can be performed through the following process. After removing the supernatant, excluding only the pellet, which is a lump of settled particles at the bottom, 5 mL of 25 mM phosphate (pH 7.4) is added. Next, dispersion is performed for about 1 minute using a tip sonicator, and centrifugation is performed.
  • casein As a blocking agent, 4 mL of casein (PBS, 1%) and 1 mL of the previously prepared solution were added, and the mixture was stirred for 15 hours using a rotator. Next, casein-latex particles were separated by centrifugation. After that, washing was repeated twice. At this time, washing can be performed through the following process. After removing the supernatant, 5 mL of 25 mM phosphate (pH 7.4) is added, excluding only the pellet, which is a lump of settled particles at the bottom. Next, dispersion is performed for about 1 minute using a tip sonicator, and centrifugation is performed.
  • a complex was prepared by first cross-linking the protein to the beads and then blocking with a blocking agent.
  • the specific manufacturing method is as follows.
  • Each of 150 ⁇ L of the complex according to Comparative Example 3-1, 150 ⁇ L of the complex according to Examples 3-1 and 3-2, and 450 ⁇ L of the sample dilution solution were mixed. Thereafter, 600 ⁇ L of the mixed solution was injected into a cuvette. 80 ⁇ L of C-peptide antibody was prepared by drying it on the rod. The cuvette and the rod were combined with the body to prepare a cartridge. Antigen calibrators were prepared at 0, 0.24, 1.2, 6, and 10 ng/mL, and 10 ⁇ L of C-peptide antigen was injected into the tip. Thereafter, the cartridge was combined with the equipment and the Optical Density was measured.
  • the protein was first cross-linked to the beads and then blocked with a blocking agent, and it was confirmed that the accuracy of turbidity analysis was reduced because the active site of the protein was covered by the blocking agent or there was no directionality upon substitution.
  • the blocking agent due to the low stability of the physically adsorbed protein, it may fall off from the beads during blocking, and there is a possibility that non-specific binding may occur due to the fallen protein.
  • the measured values in the positive control were approximately 0.1381 and 0.0799, respectively, and the antibody concentrations calculated through the calibrator were confirmed to be almost similar at 2.9 to 3.3 and 7.1 to 7.5 ng/mL, respectively. That is, it can be seen that the complex according to Example 3-2 has excellent accuracy in turbidity analysis.
  • Example 3-2 150 ⁇ L of the complex according to Example 3-2 and 450 ⁇ L of the sample dilution solution were mixed. Thereafter, 600 ⁇ L of the mixed solution was injected into a cuvette. 80 ⁇ L of C-peptide antibody was prepared by drying it on the rod. The cuvette and the rod were combined with the body to prepare a cartridge. Antigen calibrators were prepared at 0, 0.24, 1.2, 6, and 10 ng/mL, and 10 ⁇ L of C-peptide antigen was injected into the tip. Thereafter, after combining the cartridge with the equipment, the Optical Density was measured over time (0, 2, 5, 7, 14, 21, and 28 days). As a result, referring to Fig. 17, it was confirmed that the complex according to Example 3-2 did not have a significant change in %Slope over time, and it could be seen that it had excellent stability.
  • the measured values in the whole blood sample were approximately 0.1450 and 0.1037, respectively, and the concentrations calculated through the calibrator were confirmed to be almost similar at 2.4 to 2.7 and 5.4 to 5.8 ng/mL, respectively. That is, it can be seen that the complex according to Example 3-2 has excellent accuracy in turbidity analysis.

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Abstract

Un composite selon divers modes de réalisation de la présente invention comprend : des billes ; un agent de blocage qui recouvre les billes ; et une protéine qui est réticulée chimiquement avec l'agent de blocage. Une composition pour l'analyse de turbidité, selon divers modes de réalisation de la présente invention, comprend le composite. Un procédé de fabrication d'un composite selon divers modes de réalisation de la présente invention comprend les étapes consistant à : préparer des billes ; recouvrir les billes d'un agent de blocage ; et réticuler chimiquement l'agent de blocage et une protéine.
PCT/KR2024/002500 2023-02-27 2024-02-27 Composite, composition pour analyse de turbidité comprenant celui-ci, et son procédé de fabrication Ceased WO2024181766A1 (fr)

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GUTKNECHT MICHAEL F., KAKU HIROAKI, ROTHSTEIN THOMAS L.: "Microparticle immunocapture assay for quantitation of protein multimer amount and size", CELL REPORTS METHODS, vol. 2, no. 5, 1 May 2022 (2022-05-01), pages 100214, XP093204747, ISSN: 2667-2375, DOI: 10.1016/j.crmeth.2022.100214 *

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