KR102195156B1 - Antimicrobial Adhesive Composition and Method For Preparing Same - Google Patents

Abstract

The present invention relates to an antibacterial functional coating composition containing an adhesive protein containing an antimicrobial peptide and dopamine, and a method for manufacturing the same, and the antimicrobial coating composition according to the present invention requires a long time adhesion or coating which is a problem of a conventional mussel-derived adhesive. It provides a coating composition capable of exhibiting an antibacterial effect on various microorganisms or viruses such as gram-positive bacteria, gram-negative bacteria, bacteria, and fungi that are harmful to the human body while having strong adhesion in a short time.

Description

Antimicrobial Adhesive Composition and Method For Preparing Same}

The present invention relates to a coating composition capable of imparting an antimicrobial function on various substrates such as polymers, glass, metal, fabric, etc. by using an antibacterial adhesive protein. It relates to a coating composition capable of imparting an antibacterial function by coating on a substrate such as fiber or glass, and a method of manufacturing the same.

The adhesive secreted by mussels and barnacles is a water-resistant adhesive and a bio-adhesive made of protein, and is known to be harmless to the human body and not cause an immune response. In addition, since it is an adhesive made of protein, it is also an environmentally friendly adhesive that is biodegraded by the action of microorganisms or enzymes.

The mussel adhesive protein secreted from the mussel's foot is an average of 20% or more of 3,4-dihydroxyphenyl-L-alanine (L-DOPA), which is made by the hydroxylation process of the amino acid tyrosine. And DOPA is known to play a key role in the adhesion function. DOPA residues exhibit strong adhesion through crosslinking reactions between adhesion proteins through dopa-quinone converted through an oxidation process.

However, the mussel adhesive protein takes at least 12 hours or more to exhibit adhesion, and thus industrial applications are limited.

In recent years, as a method for overcoming the problem of mussel adhesion protein, an adhesion/coating technology using polydopamine imitating mussel adhesion protein or synthetic polymer in which dopamine is introduced into polyethylene glycol has been actively researched and developed.

Unlike mussel adhesive proteins, which take a long time for adhesion, polydopamine can be coated within minutes when using an appropriate solvent and oxidizing agent, and has the advantage of mass production through a chemical synthesis process, so industrial application research and development are actively progressing.

For example, Korean Patent Publication No. 10-2013-0031163 proposes a method of shortening the coating time within minutes by using an alkaline solvent by adding an oxidizing agent to polydopamine.

However, polydopamine has a high hardness including benzene ring due to its molecular structure, but has a weak impact resistance, which is easily broken by external impact.The coating composition composed of dopamine and an oxidizing agent in an alkaline solvent has a very rapid polymerization reaction, making it difficult to control the reaction. There was a problem of uneven surface coating. These problems may limit the industrial use of polydopamine.

An object of the present invention is to solve the above-described problems, it can be uniformly coated on various surfaces while the adhesive force acts quickly, and it is easy to apply industrially by improving mechanical properties such as weak impact resistance of polydopamine, and antibacterial It is to provide an antibacterial coating composition having excellent lasting power.

Another object of the present invention is to provide a method of preparing an antibacterial coating composition as described above.

In order to solve the above problems, one embodiment of the present invention, an antimicrobial peptide bonded adhesive protein; And it provides an antibacterial coating composition comprising dopamine.

In the present invention, the adhesive protein may be selected from the group consisting of an adhesive protein derived from mussels (Mussel), an adhesive protein derived from Barnacle, and combinations thereof.

In the present invention, the adhesion protein may be characterized in that the tyrosine residue is modified with dopa (DOPA) or dopa quinone.

In the present invention, it provides an antibacterial coating composition comprising the adhesive protein and dopamine in a weight ratio of 10:1 to 1:1.

The antimicrobial coating composition of the present invention may include a weakly alkaline solvent having a pH of greater than 7.0 and less than or equal to 9.0.

The solvent may be selected from sodium acetate, sodium bicarbonate, phosphate, and combinations thereof.

The antimicrobial coating composition of the present invention is one or more metals selected from the group consisting of iron (Fe ³⁺ ), chromium (Cr ⁶⁺ ), manganese (Mn ⁷⁺ ) and iodine (I ⁷⁺ ) as an oxidizing agent, hydrogen peroxide, or sodium peroxide bisulfate. (Na ₂ S ₂ O ₈ ) may be included.

In another embodiment of the present invention, mixing a solution containing an adhesive protein to which an antimicrobial peptide is bound and a solution containing dopamine; And it provides a method for producing an antibacterial coating comprising the step of applying the mixed solution on a substrate.

In the present invention, the manufacturing method may further include the step of adding an oxidizing agent to the mixed solution.

Another embodiment of the present invention provides an antimicrobial coating comprising an adhesive protein to which an antimicrobial peptide is bound and dopamine.

The antimicrobial coating composition according to the present invention improves the disadvantages of conventional mussel-derived adhesives, which require long-term adhesion or coating, and has strong adhesion in a short time, and at the same time, it is resistant to various microorganisms or viruses such as gram-positive bacteria, gram-negative bacteria, bacteria, and fungi that are harmful to the human body. It provides a coating composition that can exhibit an antibacterial effect.

In addition, the antimicrobial coating composition according to the present invention has a characteristic of long-lasting strong antibacterial activity compared to the existing technology, has processability that is easy to apply to various products, is biodegradable under certain conditions, and does not use organic solvents for coating or bonding. Because of its excellent eco-friendliness, it can be usefully used for antibacterial, antiviral, and anti-atopic adhesives for various product lines such as clothing, cosmetics, electronic devices, and medical devices.

1 shows the results of analyzing the surface of an antimicrobial coating prepared at various concentrations in a neutral solvent with an electron microscope and an alpha analyzer.
2 shows the results of analyzing the thickness of the antimicrobial coating prepared at various concentrations and coating times in a weakly alkaline solvent with an alpha meter.
3 is a result of comparing the antibacterial properties of a silicon wafer coated with the antibacterial coating composition of the present invention.

Hereinafter, embodiments of the present invention will be described in detail with reference to the drawings. The following description is only for easily understanding the embodiments of the present invention, and is not intended to limit the scope of protection.

The present invention relates to an antibacterial coating composition based on a bioadhesive, wherein the antimicrobial coating composition according to the present invention comprises: an adhesive protein to which an antimicrobial peptide is bound; And dopamine.

In the present invention, the adhesive protein means an adhesive protein capable of self-adhesive in a humid environment or a dry environment, and a protein that can be adhered or coated without adding a separate curing agent is inherently adhesive or through chemical modification. it means. Examples of commercially available self-adhesive proteins include MAPTrix™, a mussel-derived recombinant adhesive protein sold by Collodis Biosciences, North Augusta, South Carolina, or an antimicrobial adhesive protein sold by Biobit Co., Ltd. in Guro-gu, Seoul. It is not limited thereto.

According to an embodiment of the present invention, the adhesive protein usable in the present invention may be selected from the group consisting of itself or a genetically recombinant functionalized mussel-derived adhesive protein, barnacle-derived adhesive protein, and combinations thereof. I can.

In the present invention, the adhesive protein is used as such, or foot protein-3 (FP-3) described in SEQ ID NO: 1, 2, 3 or 4, SEQ ID NO: 5, 6, 7 or 8 It corresponds to the carbon-terminal or amine-terminal or both of the joxa protein-5 (FP-5) of SEQ ID NO: 9, or of the barnacle adhesive protein of SEQ ID NO: 10 The first peptide and mussel adhesion protein FP-1 (SEQ ID NOs: 11, 12, 13, 14, 15) and at least one second peptide selected from the group consisting of fragments of each protein may be used as a fusion protein. .

Preferably, the first peptide is FP-5 comprising the amino acid sequence of SEQ ID NO: 5, 6, 7 or 8 or a barnacle adhesive protein comprising the amino acid sequence of SEQ ID NO: 10, and the second peptide is SEQ ID NO: 12 Or FP-1 comprising an amino acid sequence of 14. More preferably, the adhesive protein usable in the present invention is FP-1 comprising the amino acid sequence of SEQ ID NO: 11, 12, or 14.

In the present invention, it is preferable that the adhesive protein has a form in which an antimicrobial peptide is added to the nitrogen or carbon terminus of an adhesive protein existing in nature or an adhesive protein designed recombinantly.

In the case of the antimicrobial peptide added to the adhesive protein in the present invention, a peptide exhibiting antimicrobial function derived from nature or artificially synthesized may be used. Antibacterial peptides exert an antibacterial effect through a mechanism that destroys the cell membrane of microorganisms or inhibits metabolic function by penetrating the cell membrane. In the present invention, all antimicrobial peptides exhibiting antibacterial effects as a mechanism for destroying the cell membrane of microorganisms are included. Preferably, the antimicrobial peptide to be added to the adhesive protein may be selected from antimicrobial peptides effective against gram-positive bacteria as well as gram-negative bacteria.

For example, preferred antimicrobial peptides usable in the present invention are KLWKKWAKKWLKLWKA (SEQ ID NO: 16), FALALKALKKL (SEQ ID NO: 17), ILRWPWWPWRRK (SEQ ID NO: 18), AKRHHGYKRKFH (SEQ ID NO: 19), KWKLFKKIGAVLKVL (SEQ ID NO: 20) SEQ ID NO: 21), IWSILAPLGTTLVKLVAGIGQQKRK (SEQ ID NO: 22), GIGAVLKVLTTGLPALISWI (SEQ ID NO: 23), SWLSKTAKKGAVLKVL (SEQ ID NO: 24), KKLFKKILKYL (SEQ ID NO: 25), GLKKLISWIKRAAQQQG (SEQ ID NO: 27) GLKKLISWIKRAAQQQG (SEQ ID NO: 27), GLKQLAKKTIQ, 28), KLLLKLLKKLLKLLKKK (SEQ ID NO: 29), THRPPMWSPVWP (SEQ ID NO: 30), GWLKKIGKWKIFKK (SEQ ID NO: 31), ILPWKWPWWPWRR (SEQ ID NO: 32), RRWWCRC (SEQ ID NO: 33), KLAKLAKLAKLAKLAK (SEQ ID NO: 34WPLAKLAKLAK and SEQ ID NO: Number 35).

In the present invention, the mussel adhesion protein may change a tyrosine residue among the constituent amino acids to DOPA or dopaquinone through chemical modification. The modified waveguide and dopaquinone can play a very important role in adhesion to the surface. Chemical modification of the genetically modified mussel adhesion protein can be performed using a mushroom-derived tyrosinase enzyme that can mediate it. The antimicrobial mussel adhesive protein that has undergone chemical modification can be attached to various materials such as metal, plastic, and glass without limitation.

The antibacterial coating composition provided by the present invention may include dopamine together with the antibacterial adhesive protein.

The dopamine has a chemical structure including an alkylamine and a catechol functional group, as shown in Formula 1 below, wherein the alkylamine is similar to lysine, and the catechol is Similar to L-DOPA. Such dopamine is a substance having strong adhesion on organic or inorganic substances.

In the present invention, it was found that when the adhesive protein to which the antimicrobial peptide is bound is mixed with dopamine, the conventional surface coating time, which takes several hours, can be shortened to within several minutes. In the case of pure dopamine, if the surface is coated alone, the antimicrobial effect is not uniform over the entire surface as the coating surface is not uniform. However, when used in combination with adhesive protein, the surface coating is relatively uniform and a certain quality of antibacterial effect can be achieved. have.

In the present invention, the antimicrobial coating composition may include the adhesive protein and dopamine in a mass ratio of 10:1 to 1:1, preferably 10:1 to 5:1, and more preferably 10:1 to 8: It can be included in a mass ratio of 1. When the dopamine is used in a ratio lower than 10:1, the ratio that mediates the reaction between the adhesive protein and the surface decreases, and as a result, a partially uncoated surface may be obtained, thereby reducing the uniformity of the coating, resulting in antibacterial effect There may be an inconsistent problem, and if it is used more than 1:1, the self-polymerization ratio of dopamine increases and the ratio of dopamine that participates in crosslinking with the antibacterial adhesive protein decreases. The rate of coating on the surface is also reduced, and as a result, the problem of decreasing the antimicrobial coated surface may occur.

The antibacterial coating composition according to the present invention may further include a solvent for mixing the adhesive protein and dopamine. The solvent usable in the present invention may be any water-soluble solvent having a pH of 4.0 to 10.0, and in particular, for rapid coating, it is preferable to use a weakly alkaline solvent (pH greater than 7.0 and less than or equal to 9.0). In the present invention, a preferred solvent for preparing a weakly alkaline solvent may freely use a material that can satisfy the above pH range, for example, sodium acetate, sodium bicarbonate, and phosphite ( phosphate) may be used, and a mixed solvent of sodium acetate and sodium hydrogen carbonate may be preferably used in the present invention.

In the present invention, the mixture of the adhesive protein and dopamine may be mixed in a solvent at a concentration of 0.1 to 10 mg/mL, and preferably at a concentration of 0.5 to 2 mg/mL. In one embodiment of the present invention, it was confirmed that the coating composition having a concentration within the numerical range has an even coating thickness distribution.

The antibacterial coating composition according to the present invention may further include an oxidizing agent. The oxidizing agent is one or more metals selected from the group consisting of iron (Fe ³⁺ ), chromium (Cr ⁶⁺ ), manganese (Mn ⁷⁺ ) and iodine (I ⁷⁺ ), hydrogen peroxide, or sodium bisulfate peroxide (Na ₂ S ₂ O ₈ ) may be used, wherein the oxidizing agent may be contained in an amount of 0.01 to 5 parts by weight based on the total weight of the dopamine.

The antimicrobial coating composition according to the present invention provides a coating composition capable of exhibiting an antibacterial effect against various microorganisms or viruses at the same time having strong adhesion in a short time by improving the disadvantage of long-term adhesion or coating, which is a problem of mussel-derived adhesives composed of pure protein do.

The molecular skeleton of the antimicrobial adhesive according to a preferred embodiment of the present invention has amphiphilic properties and can be used as an additive to existing antimicrobial coating products, and the antibacterial adhesive can be used as a water-soluble or oil-soluble coating agent. The antimicrobial coating composition according to the present invention has a characteristic that a strong antibacterial activity lasts for a long time compared to the existing technology, and at the same time, it has durability that the antibacterial coating agent is not easily damaged by external environment or pressure. In addition, it has processability that is easy to apply to various products, is biodegradable under certain conditions, and has excellent eco-friendliness that does not use organic solvents during coating or bonding, and is used for antibacterial, antiviral, and anti-atopic adhesives for various product lines. Can be used usefully.

The present invention also comprises the steps of preparing a mixed solution by dissolving the antimicrobial peptide-bound adhesive protein and dopamine in a solvent; And it provides a method for producing an antimicrobial functional coating comprising the step of applying the mixed solution on a substrate.

The antimicrobial coating composition of the present invention may be coated using a known coating method. For example, as a first step, the adhesive protein is dissolved in a sodium acetate buffer solution having a pH of 5.0 to 6.0 at a concentration of 10 mg/mL or higher, and then diluted with a weakly alkaline buffer having a pH of 7 to 9 to obtain a coating concentration of 0.1 mg/mL. .

As a second step, dopamine is dissolved in a sodium acetate buffer having a pH of 5.0 to 6.0 at a concentration of 10 mg/mL, diluted to a concentration of 0.05 mg/mL with a weak alkaline buffer, and then added to a weak alkaline solution in which the adhesive protein is dissolved.

As a final step, sodium periodate is prepared in a weak alkaline buffer at a concentration of 0.01 mg/mL, added to the adhesive protein/dopamine mixed solution, and then uniformly mixed and applied on the substrate to prepare an antibacterial functional coating.

The substrate applicable in the present invention may be a metal, plastic, glass, composite material, a material derived from a living body, a hybrid material composed of a biological material and a synthetic material, and the like. In addition, the surface to which the present invention is applied may impart antibacterial functions to various surfaces such as a flat surface, a concave surface, a porous surface, and a spherical surface.

Example

Hereinafter, the present invention will be described in more detail through examples. These examples are for illustrative purposes only, and it will be apparent to those of ordinary skill in the art that the scope of the present invention is not to be construed as being limited by these examples.

Preparation Example 1: Antimicrobial peptide binding-genetic recombinant mussel adhesive protein preparation

For the production of mussel adhesive protein with antimicrobial peptide conjugated, a genetic sequence with an antimicrobial peptide sequence added to the C-terminal or N-terminal region of the mussel adhesive protein MAPTrix™ was designed and produced by Kozmo Gentech (Seoul, Korea). I requested. The added sequence is shown in Table 1 below.

Fusion peptide order Fusion site A KLWKKWAKKWLKLWKA C-terminal B ILRWPWWPWRRK C-terminal C FALALKALKKL C-terminal

The mussel adhesive protein bound with the antimicrobial peptide was dissolved in 0.1M sodium acetate buffer at a concentration of 1 mg/ml, and oxygen gas was injected to saturate oxygen in the surface-active adhesive protein solution for 30 minutes. Thereafter, tyrosinase was added at a concentration of 5 μg per 1 mg of antimicrobial adhesive protein, followed by stirring for 1 hour while injecting oxygen. After 1 hour, 5% acetic acid was added to terminate the chemical modification reaction. The adhesive protein solution after the reaction was lyophilized to obtain a powder. Through the above process, a mussel adhesive protein in which the tyrosine residue was modified with DOPA was obtained.

Preparation Example 2: Preparation of antibacterial coating composition and antibacterial functional coating

1 mg of the adhesive protein obtained in Preparation Example 1 and 0.1 mg of dopamine were each dissolved in a solvent, and the two solutions were mixed to prepare an antibacterial coating composition solution.

As the solvent, demineralized water of pH 7 and sodium acetate of pH 8 were used to match the examples below.

Sodium peroxide bisulfate (Na ₂ S ₂ O ₈ ) as an oxidizing agent was added to the prepared sample by 1 part by mass based on dopamine to prepare an antibacterial coating composition.

A silicon wafer specimen was placed on the surface of a polystyrene microwell plate, and 1 mL of the prepared coating composition was applied to the specimen using a pipette to perform surface coating.

After the coating was completed, the coating solution was removed, the surface was washed with distilled water, and the surface was dried on a clean bench to prepare a silicon wafer coated with an antibacterial adhesive protein.

Example 1. Analysis of the coating surface

1-1: Analysis of the coating surface in a neutral solvent

Silicon wafer for 30 minutes in a neutral (pH 7) solvent with a mixed solution of antimicrobial mussel adhesive protein/dopamine having a weight ratio of 10/1 at coating concentrations of 0.1 mg/mL, 0.5 mg/mL, 1.0 mg/mL and 2.0 mg/mL The result of coating the surface was observed with an electron microscope, and the result of measuring the coating thickness with an alpha step measuring device (Surface Profiler, DektakXT, USA Bruker) is shown in FIG. 1.

As can be seen in FIG. 1, in a neutral solvent, the sample having a concentration of 2.0 mg/mL of an adhesive protein/dopamine mixture was coated with a relatively uniform surface (FIG. 1(d)), but at a concentration below that It can be seen that a non-uniform coating was formed (FIGS. 1(a) to (c)).

1-2: Analysis of coating surface in weakly alkaline solvent

Antimicrobial by coating a silicone wafer with a coating concentration of 0.5mg/mL and 1.0mg/mL in a weak alkaline (pH 8) solvent with a weight ratio of antimicrobial mussel adhesive protein/dopamine of 10/1 and coating a silicon wafer for 30 minutes and 1 hour, respectively. A functional coating was obtained. The result of measuring the coating thickness of the obtained coating with an alpha meter is shown in FIG. 2.

In FIG. 2, it can be seen that the surface coating was relatively uniformly performed even at a low concentration (0.5 mg/mL) under a weakly alkaline solvent.

In addition, it was confirmed that even when the coating time was lengthened to 1 hour in order to increase the coating thickness, a coating layer having a uniform thickness over the entire surface could be formed. The coating thickness increased proportionally with the concentration of the coating solution.

Example 2: Measurement of antibacterial effect of antibacterial functional coating

The antibacterial effect was tested for the antimicrobial functional coating of 0.5mg/mL prepared in Example 1-2.

After diluting the previously cultured Staphylococcus aureus ( S. Aureus ) with PBS to 10 ⁴ CFU/ml, the antimicrobial effect was obtained by inoculating Staphylococcus aureus on the coated silicon wafer and the non-coated silicon wafer respectively. Comparative measurements were made.

As shown in FIG. 3, as a result of measuring the antibacterial activity of the wafer coated with the antibacterial coating composition of the present invention, it was confirmed that the antibacterial effect was about 90% or more despite the hard surface regardless of time.

<110> Biovit Co., Ltd. <120> Antimicrobial Adhesive Composition and Method For Preparing Same <130> JPN18002 <160> 35 <170> KoPatentIn 3.0 <210> 1 <211> 52 <212> PRT <213> Artificial Sequence <220> <223> Foot protein type 3 (FP-3, Mytilus edulis) <400> 1 Ala Asp Tyr Tyr Gly Pro Lys Tyr Gly Pro Pro Arg Arg Tyr Gly Gly 1 5 10 15 Gly Asn Tyr Asn Arg Tyr Gly Gly Ser Arg Arg Tyr Gly Gly Tyr Lys 20 25 30 Gly Trp Asn Asn Gly Trp Lys Arg Gly Arg Trp Gly Arg Lys Tyr Tyr 35 40 45 Glu Phe Glu Phe 50 <210> 2 <211> 46 <212> PRT <213> Artificial Sequence <220> <223> Foot protein type 3 (FP-3, Mytilus galloprovincialis: mgfp-3A) <400> 2 Ala Asp Tyr Tyr Gly Pro Lys Tyr Gly Pro Pro Arg Arg Tyr Gly Gly 1 5 10 15 Gly Asn Tyr Asn Arg Tyr Gly Arg Arg Tyr Gly Gly Tyr Lys Gly Trp 20 25 30 Asn Asn Gly Trp Lys Arg Gly Arg Trp Gly Arg Lys Tyr Tyr 35 40 45 <210> 3 <211> 50 <212> PRT <213> Artificial Sequence <220> <223> Foot protein type 3 (FP-3, Mytilus edulis: mefp-3F) <400> 3 Ala Asp Tyr Tyr Gly Pro Asn Tyr Gly Pro Pro Arg Arg Tyr Gly Gly 1 5 10 15 Gly Asn Tyr Asn Arg Tyr Asn Gly Tyr Gly Gly Gly Arg Arg Tyr Gly 20 25 30 Gly Tyr Lys Gly Trp Asn Asn Gly Trp Asn Arg Gly Arg Arg Gly Lys 35 40 45 Tyr Trp 50 <210> 4 <211> 44 <212> PRT <213> Artificial Sequence <220> <223> Foot protein type 3 (FP-3, Mytilus californianus) <400> 4 Gly Ala Tyr Lys Gly Pro Asn Tyr Asn Tyr Pro Trp Arg Tyr Gly Gly 1 5 10 15 Lys Tyr Asn Gly Tyr Lys Gly Tyr Pro Arg Gly Tyr Gly Trp Asn Lys 20 25 30 Gly Trp Asn Lys Gly Arg Trp Gly Arg Lys Tyr Tyr 35 40 <210> 5 <211> 75 <212> PRT <213> Artificial Sequence <220> <223> Foot protein type 5 (FP-5, Mytilus edulis) <400> 5 Ser Ser Glu Glu Tyr Lys Gly Gly Tyr Tyr Pro Gly Asn Ala Tyr His 1 5 10 15 Tyr His Ser Gly Gly Ser Tyr His Gly Ser Gly Tyr His Gly Gly Tyr 20 25 30 Lys Gly Lys Tyr Tyr Gly Lys Ala Lys Lys Tyr Tyr Tyr Lys Tyr Lys 35 40 45 Asn Ser Gly Lys Tyr Lys Tyr Leu Lys Lys Ala Arg Lys Tyr His Arg 50 55 60 Lys Gly Tyr Lys Lys Tyr Tyr Gly Gly Ser Ser 65 70 75 <210> 6 <211> 76 <212> PRT <213> Artificial Sequence <220> <223> Foot protein 5 (FP-5, Mytilus edulis) <400> 6 Ser Ser Glu Glu Tyr Lys Gly Gly Tyr Tyr Pro Gly Asn Thr Tyr His 1 5 10 15 Tyr His Ser Gly Gly Ser Tyr His Gly Ser Gly Tyr His Gly Gly Tyr 20 25 30 Lys Gly Lys Tyr Tyr Gly Lys Ala Lys Lys Tyr Tyr Tyr Lys Tyr Lys 35 40 45 Asn Ser Gly Lys Tyr Lys Tyr Leu Lys Lys Ala Arg Lys Tyr His Arg 50 55 60 Lys Gly Tyr Lys Lys Tyr Tyr Gly Gly Gly Ser Ser 65 70 75 <210> 7 <211> 71 <212> PRT <213> Artificial Sequence <220> <223> Foot protein 5 (FP-5, Mytilus coruscus) <400> 7 Tyr Asp Asp Tyr Ser Asp Gly Tyr Tyr Pro Gly Ser Ala Tyr Asn Tyr 1 5 10 15 Pro Ser Gly Ser His Trp His Gly His Gly Tyr Lys Gly Lys Tyr Tyr 20 25 30 Gly Lys Gly Lys Lys Tyr Tyr Tyr Lys Phe Lys Arg Thr Gly Lys Tyr 35 40 45 Lys Tyr Leu Lys Lys Ala Arg Lys Tyr His Arg Lys Gly Tyr Lys Lys 50 55 60 His Tyr Gly Gly Ser Ser Ser 65 70 <210> 8 <211> 76 <212> PRT <213> Artificial Sequence <220> <223> Foot protein 5 (FP-5, Mytilus galloprovincialis) <400> 8 Ser Ser Glu Glu Tyr Lys Gly Gly Tyr Tyr Pro Gly Asn Thr Tyr His 1 5 10 15 Tyr His Ser Gly Gly Ser Tyr His Gly Ser Gly Tyr His Gly Gly Tyr 20 25 30 Lys Gly Lys Tyr Tyr Gly Lys Ala Lys Lys Tyr Tyr Tyr Lys Tyr Lys 35 40 45 Asn Ser Gly Lys Tyr Lys Tyr Leu Lys Lys Ala Arg Lys Tyr His Arg 50 55 60 Lys Gly Tyr Lys Lys Tyr Tyr Gly Gly Gly Ser Ser 65 70 75 <210> 9 <211> 99 <212> PRT <213> Artificial Sequence <220> <223> Foot protein 6 (FP-6, Mytilus edulis) <400> 9 Gly Gly Gly Asn Tyr Arg Gly Tyr Cys Ser Asn Lys Gly Cys Arg Ser 1 5 10 15 Gly Tyr Ile Phe Tyr Asp Asn Arg Gly Phe Cys Lys Tyr Gly Ser Ser 20 25 30 Ser Tyr Lys Tyr Asp Cys Gly Asn Tyr Ala Gly Cys Cys Leu Pro Arg 35 40 45 Asn Pro Tyr Gly Arg Val Lys Tyr Tyr Cys Thr Lys Lys Tyr Ser Cys 50 55 60 Pro Asp Asp Phe Tyr Tyr Tyr Asn Asn Lys Gly Tyr Tyr Tyr Tyr Asn 65 70 75 80 Asp Lys Asp Tyr Phe Asn Cys Gly Ser Tyr Asn Gly Cys Cys Leu Arg 85 90 95 Ser Gly Tyr <210> 10 <211> 56 <212> PRT <213> Artificial Sequence <220> <223> Semibalanus balanoides <400> 10 Met Arg Val Ile Leu Phe Ala Met Leu Ile Gly Gly Ser Leu Ala Cys 1 5 10 15 Gln Asn Arg Leu Glu Thr Leu Val Gln Glu Ala Thr Gly Asn Ala Gly 20 25 30 Asp Leu Ser Thr Asn Val His Glu Glu Cys Asn Ser Gln Val Gly Thr 35 40 45 Phe Asn Ala Val His Ala Pro Gln 50 55 <210> 11 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> Decapeptide (FP-1, Mytilus edulis) <400> 11 Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys 1 5 10 <210> 12 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> 2 time repeated decapeptide (FP-1, Mytilus edulis) <400> 12 Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro 1 5 10 15 Pro Thr Tyr Lys 20 <210> 13 <211> 30 <212> PRT <213> Artificial Sequence <220> <223> 3 times repeated decapeptide (FP-1, Mytilus edulis) <400> 13 Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro 1 5 10 15 Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys 20 25 30 <210> 14 <211> 40 <212> PRT <213> Artificial Sequence <220> <223> 4 times repeated decapeptide (FP-1, Mytilus edulis) <400> 14 Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro 1 5 10 15 Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys 20 25 30 Pro Ser Tyr Pro Pro Thr Tyr Lys 35 40 <210> 15 <211> 60 <212> PRT <213> Artificial Sequence <220> <223> 6 times repeated decapeptide (FP-1, Mytilus edulis) <400> 15 Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro 1 5 10 15 Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys 20 25 30 Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr 35 40 45 Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys 50 55 60 <210> 16 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (KLWKKWAKKWLKLWKA) <400> 16 Lys Leu Trp Lys Lys Trp Ala Lys Lys Trp Leu Lys Leu Trp Lys Ala 1 5 10 15 <210> 17 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (FALALKALKKL) <400> 17 Phe Ala Leu Ala Leu Lys Ala Leu Lys Lys Leu 1 5 10 <210> 18 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (ILRWPWWPWRRK) <400> 18 Ile Leu Arg Trp Pro Trp Trp Pro Trp Arg Arg Lys 1 5 10 <210> 19 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (AKRHHGYKRKFH) <400> 19 Ala Lys Arg His His Gly Tyr Lys Arg Lys Phe His 1 5 10 <210> 20 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (KWKLFKKIGAVLKVL) <400> 20 Lys Trp Lys Leu Phe Lys Lys Ile Gly Ala Val Leu Lys Val Leu 1 5 10 15 <210> 21 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (LVKLVAGIKKFLKWK) <400> 21 Leu Val Lys Leu Val Ala Gly Ile Lys Lys Phe Leu Lys Trp Lys 1 5 10 15 <210> 22 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (IWSILAPLGTTLVKLVAGIGQQKRK) <400> 22 Ile Trp Ser Ile Leu Ala Pro Leu Gly Thr Thr Leu Val Lys Leu Val 1 5 10 15 Ala Gly Ile Gly Gln Gln Lys Arg Lys 20 25 <210> 23 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (GIGAVLKVLTTGLPALISWI) <400> 23 Gly Ile Gly Ala Val Leu Lys Val Leu Thr Thr Gly Leu Pro Ala Leu 1 5 10 15 Ile Ser Trp Ile 20 <210> 24 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (SWLSKTAKKGAVLKVL) <400> 24 Ser Trp Leu Ser Lys Thr Ala Lys Lys Gly Ala Val Leu Lys Val Leu 1 5 10 15 <210> 25 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (KKLFKKILKYL) <400> 25 Lys Lys Leu Phe Lys Lys Ile Leu Lys Tyr Leu 1 5 10 <210> 26 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (GLKKLISWIKRAAQQG) <400> 26 Gly Leu Lys Lys Leu Ile Ser Trp Ile Lys Arg Ala Ala Gln Gln Gly 1 5 10 15 <210> 27 <211> 39 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (GWLKKIGKKIERVGQHTRDATIQGLGIAQQAANVAATAR) <400> 27 Gly Trp Leu Lys Lys Ile Gly Lys Lys Ile Glu Arg Val Gly Gln His 1 5 10 15 Thr Arg Asp Ala Thr Ile Gln Gly Leu Gly Ile Ala Gln Gln Ala Ala 20 25 30 Asn Val Ala Ala Thr Ala Arg 35 <210> 28 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (LKKLAKLALAF) <400> 28 Leu Lys Lys Leu Ala Lys Leu Ala Leu Ala Phe 1 5 10 <210> 29 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (KLLLKLLKKLLKLLKKK) <400> 29 Lys Leu Leu Leu Lys Leu Leu Lys Lys Leu Leu Lys Leu Leu Lys Lys 1 5 10 15 Lys <210> 30 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (THRPPMWSPVWP) <400> 30 Thr His Arg Pro Pro Met Trp Ser Pro Val Trp Pro 1 5 10 <210> 31 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (GWLKKIGKWKIFKK) <400> 31 Gly Trp Leu Lys Lys Ile Gly Lys Trp Lys Ile Phe Lys Lys 1 5 10 <210> 32 <211> 13 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (ILPWKWPWWPWRR) <400> 32 Ile Leu Pro Trp Lys Trp Pro Trp Trp Pro Trp Arg Arg 1 5 10 <210> 33 <211> 7 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (RRWWCRC) <400> 33 Arg Arg Trp Trp Cys Arg Cys 1 5 <210> 34 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (KLAKLAKKLAKLAK) <400> 34 Lys Leu Ala Lys Leu Ala Lys Lys Leu Ala Lys Leu Ala Lys 1 5 10 <210> 35 <211> 23 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (LKKLAKLALAFILRWPWWPWRRK) <400> 35 Leu Lys Lys Leu Ala Lys Leu Ala Leu Ala Phe Ile Leu Arg Trp Pro 1 5 10 15 Trp Trp Pro Trp Arg Arg Lys 20

Claims (11)

Adhesion protein to which antimicrobial peptides are bound; And as an antibacterial coating composition comprising dopamine in a weight ratio of 10:1 to 8:1,
The adhesive protein is selected from the group consisting of mussel (Mussel)-derived adhesive protein, barnacle-derived adhesive protein, and combinations thereof. delete The method of claim 1,
The adhesion protein is characterized in that the tyrosine residue is modified with dopa (DOPA) or dopa quinone, antibacterial coating composition. delete The method of claim 1,
An antimicrobial coating composition further comprising a solvent of more than pH 7.0 and less than or equal to 9.0. The method of claim 5,
The antibacterial coating composition, characterized in that the solvent is selected from sodium acetate, sodium bicarbonate, phosphate, and combinations thereof. The method of claim 1,
At least one metal selected from the group consisting of iron (Fe ³⁺ ), chromium (Cr ⁶⁺ ), manganese (Mn ⁷⁺ ) and iodine (I ⁷⁺ ), hydrogen peroxide and sodium peroxide disulfate (Na ₂ S ₂ O ₈ ) An antibacterial coating composition further comprising an oxidizing agent selected from the group consisting of. Preparing a mixed solution by dissolving the antimicrobial peptide-bound adhesive protein and dopamine in a solvent at a weight ratio of 10:1 to 8:1; And
Applying the mixed solution on a substrate
As a method for producing an antibacterial coating comprising a,
The adhesive protein is selected from the group consisting of mussel-derived adhesive protein, barnacle-derived adhesive protein, and combinations thereof. The method of claim 8,
At least one metal selected from the group consisting of iron (Fe ³⁺ ), chromium (Cr ⁶⁺ ), manganese (Mn ⁷⁺ ), and iodine (I ⁷⁺ ), hydrogen peroxide, and sodium peroxide bisulfate (Na ₂ S ₂ ) in the mixed solution O ₈ ) Method for producing an antibacterial coating further comprising the step of adding an oxidizing agent selected from the group consisting of. The method of claim 8,
The method for producing an antimicrobial coating, characterized in that the solvent has a pH range of more than 7.0 and 9.0 or less. An antimicrobial coating prepared by the method of any one of claims 8 to 10.

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