KR102424889B1 - Biofunctional Adhesive Composition - Google Patents

Abstract

The present invention relates to a physiologically functional adhesive protein in which a physiologically functional peptide is bound to the C-terminus or N-terminus of an acrylated adhesive protein, and to a physiologically functional adhesive composition comprising the physiologically functional adhesive protein. The physiologically functional adhesive protein of the present invention can be coated on the surface of a mobile phone liquid crystal protective film, food packaging material, medical device, etc. to secure stability against harmful microorganisms. In particular, the physiologically functional adhesive protein of the present invention has antibacterial properties based on strong adhesion By continuously maintaining this, it is possible to effectively prevent the decrease in antimicrobial activity due to the elution of the antimicrobial substance.

Description

Biofunctional Adhesive Composition {Biofunctional Adhesive Composition}

The present invention relates to a physiologically functional adhesive composition and a method for preparing the same. More particularly, it relates to a physiologically functional adhesive composition having improved adhesion or coating properties by introducing an acrylate group into the molecular backbone of the mussel adhesive protein, and a method for preparing the same. In the mussel adhesive protein, various functional peptides such as antibacterial, antiviral, anti-atopic, etc. may be fused between C-terminal, N-terminal, or hybrid mussel adhesive proteins.

In household items or home appliances used on a daily basis, harmful bacteria or viruses easily multiply due to the surrounding environment such as dust, saliva, and oil. In addition, industrial products such as food packaging materials, storage containers, toothbrushes, cutting boards, stationery, cosmetics and packaging materials and medical supplies due to high interest in environmental hygiene and the advancement of lifestyles due to the emergence of resistant bacteria such as avian influenza virus and super bacteria The production and demand for products that have been given various functionalities such as antibacterial properties to petrochemical materials used as products are increasing.

In the case of antibacterial agents, conventional technologies have an antibacterial effect by adding an antibiotic to a synthetic polymer or natural material or by providing a chemical environment that microorganisms do not like (Patent Document 1). However, these conventional antibacterial agents have a problem in the continuity of the antibacterial activity because the antibacterial component is gradually removed during use. In addition, the existing antibacterial technology mainly uses silver nanoparticles or inorganic particles, and there has been a debate about the harmfulness of the human body due to the departure of the fine particles, and thus the demand for an eco-friendly antibacterial technology is increasing.

In addition, organic antibacterial substances such as benzimidazole or natural antibacterial substances such as horseradish extract are simply added to the material to produce antibacterial materials (Patent Document 1 and Patent Document 2), but the toxicity and antibacterial properties of organic antibacterial substances Technical limitations such as elution of substances and reduction in antibacterial activity are pointed out (Non-Patent Document 1), and in particular, when plastics are injected or extruded, antimicrobial substances also cause thermal decomposition and yellowing. Moreover, when the antibacterial film is packaged with food, there has been a problem that serious side effects such as inducing resistance of microorganisms due to the elution of the above-mentioned antibacterial material may occur.

Accordingly, methods have been devised to improve antibacterial durability by immobilizing an antimicrobial agent or developing a substance whose chemical structure kills bacteria or a material that bacteria cannot adhere to the surface as an antibacterial agent (Patent Document 3, Non-Patent Document 2, Non-Patent Document) Literature 3). In addition, antibacterial technologies including two or more antibacterial agents have been developed to impart a wide range of antimicrobial activity (Patent Document 4), but it is insufficient to solve the problems of the prior art as described above.

Korean Patent Publication No. KR 10-2009-0024467 Korean Patent Publication No. KR 10-2008-0110578 Korean Patent Publication No. KR 10-2008-0039460 Korean Patent Publication No. KR 10-2003-0006509

K. Glinel et al., Acta Biomaterialia, 8, 1670 (2012) Mo S, Krunic A, et al., J Nat Prod. 2009 72(11):2043-5 Bin Wang, et al., Journal of Applied Polymer Science, 130(5), p3489-3497, 2013

The present invention is to solve the problems of the prior art as described above, and the present invention has an excellent coating power on various surfaces, but generally requires an adhesion time of 6 hours or more for a long time. Or for the purpose of providing a coating composition.

In addition, an antibacterial, antiviral, anti-atopic, anticancer adhesive protein in which various functional peptides such as antibacterial, anti-atopic, and antiviral are fused to the C-terminus or N-terminus of the adhesive protein, and a coating or adhesive composition containing the same aim to

In the present invention, the functional peptide refers to a substance having three or more amino acids capable of performing various physiological functions, such as antibacterial, anticancer, anti-immune, antiviral, anti-atopic, and antithrombotic, but is not necessarily limited thereto. .

In addition, the present invention chemically modifies the tyrosine residue of the mussel adhesive protein with DOPA (3,4-dihydroxyphenylalanine) and introduces an acrylate group, so that various functional surface coatings are possible in a simple way, and the use of an organic solvent as a water-soluble coating composition It aims to develop an environmentally friendly coating material that can sustain coating for a long time in harsh conditions without

Another object of the present invention is to provide a photocurable antibacterial coating material that can be applied to various materials such as liquid crystal films and home appliances by introducing a photocurable acrylate.

Certain advantages and novel features of the present invention will become more apparent from the following detailed description and preferred embodiment taken in conjunction with the accompanying drawings.

The present invention relates to an acrylated adhesive protein in which an acrylate group is introduced into an adhesive protein in which a functional peptide capable of performing antibacterial, antiviral, and anti-atopic functions is genetically engineered to an adhesive protein capable of self-adhesion in a humid or dry environment. and an adhesive or coating composition based thereon.

In addition, the present invention provides a physiologically functional adhesive protein in which a physiologically functional peptide is bound to the C-terminus or N-terminus of the acrylated adhesive protein.

In addition, the present invention provides an adhesive protein having excellent physiological functionality by adding at least one functional peptide to the C-terminus and N-terminus of the adhesive protein.

According to one embodiment of the present invention, it is possible to provide a physiologically functional coating material that can be easily coated on various surfaces by replacing the tyrosine portion of the adhesion protein to which the physiologically functional peptide is added with DOPA and introducing an acrylate group.

In addition, the present invention provides an adhesive or coating composition based on an adhesive protein into which a photocurable acrylate is introduced.

Hereinafter, the present invention will be described in detail.

The present invention provides a physiologically functional adhesive protein in which a physiologically functional peptide is bound to the C-terminus or N-terminus of the acrylate-attached adhesive protein. According to one embodiment of the present invention, the adhesion protein is preferably, but not limited to, a mussel-derived adhesion protein.

The present invention has a strong adhesive force in a short time and has an effect on various microorganisms or viruses by improving the disadvantage of requiring long-term adhesion or coating, which is a problem of mussel-derived adhesives composed only of pure protein. The molecular skeleton of the antibacterial adhesive provided in one embodiment of the present invention has an amphipathic property, so it can be used as an additive to an existing antibacterial coating product, and the antibacterial adhesive can be used as a water-soluble or oil-soluble coating agent. The antibacterial composition presented in the present invention has a long-lasting, strong antibacterial activity compared to the existing technology, and at the same time has durability that the antibacterial coating agent is not easily damaged by external environment or pressure. The physiologically functional adhesive composition of the present invention has excellent processability to be applied to various products, biodegradation under specific conditions, and eco-friendliness that does not use organic solvents for coating or bonding, and thus provides antibacterial, antiviral, and antibacterial properties for various product groups. It can be usefully used for applications such as atopic adhesives.

The present invention provides a functional coating composition comprising an adhesive protein alone or a mixture of the adhesive protein and a photocurable acrylate-based adhesive resin. The adhesive composition provided in the present invention is composed of an adhesive protein functionalized with a naturally occurring or artificially synthesized peptide. The basic structure of the adhesive protein is composed of X-P-Y, where X and Y are physiologically functional peptides, and P is an acrylated adhesive protein. In some cases, any one of X and Y may be omitted. The adhesive protein may be used without limitation as an adhesive material for any product.

The adhesive protein included in the physiologically functional adhesive composition of the present invention may include any protein capable of self-adhesion without limitation. Self-adhesive proteins include proteins that have essentially adhesive properties or have adhesive properties added through chemical modification. Examples of commercially available self-adhesive proteins include, but are not limited to, MAPTrix™, a mussel-derived recombinant adhesive protein marketed by Collodis Biosciences, North Augusta, SC. An example of an adhesive protein to which adhesion is added through chemical modification may include a protein modified with an acrylate. Examples include, but are not limited to, acrylated collagen or mussel adhesion proteins. In one embodiment of the present invention, there is provided an antimicrobial coating composition comprising an acrylated mussel adhesive protein.

In the present invention, the mussel-derived adhesion protein comprises a foot protein-1 (FP-1) having an amino acid sequence selected from the group consisting of SEQ ID NOs: 1 to 3, and the amino acid sequence of SEQ ID NO: 4 FP-2 having an amino acid sequence selected from the group consisting of SEQ ID NO: 5 to SEQ ID NO: 8, FP-4 having the amino acid sequence of SEQ ID NO: 9, selected from the group consisting of SEQ ID NO: 10 to SEQ ID NO: 13 FP-5 having an amino acid sequence that is, FP-6 having an amino acid sequence set forth in SEQ ID NO: 14, FP-151 having an amino acid sequence selected from the group consisting of SEQ ID NOs: 15 to 17, amino acids consisting of SEQ ID NO: 18 It may be selected from the group consisting of FP-131 having the sequence and FP-251 having the amino acid sequence of SEQ ID NO: 19 and fragments of each protein, but is not limited thereto.

MAPTrix™ provided in one embodiment of the present invention is a recombinantly functionalized mussel adhesion protein. In the present invention, the mussel adhesive protein is used as such, or FP-5 having the amino acid sequence shown in SEQ ID NO: 10, 11, 12 or 13 or the amino acid sequence shown in SEQ ID NO: 5, 6, 7 or 8 FP-3 having the amino acid sequence shown in SEQ ID NO: 14, the first peptide corresponding to the C-terminus, the N-terminus or both of FP-6 having the amino acid sequence set forth in SEQ ID NO: 14, and the mussel adhesion protein FP-1 (SEQ ID NO: 1), FP At least one second peptide selected from the group consisting of -2 (SEQ ID NO: 4), FP-4 (SEQ ID NO: 9) and 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: 10, 11, 12 or 13, and the second peptide is FP-1 comprising the amino acid sequence of SEQ ID NO: 1, 2 or 3 to be. In the present invention, functional peptides are required to add various physiological functions to the mussel adhesion protein.

In the present invention, the physiologically functional peptide may be a peptide having a function of destroying the cell membrane by acting on the cell membrane. According to one embodiment of the present invention, the physiologically functional peptide may be selected from the group consisting of antibacterial peptides, antiviral peptides, anticancer peptides, antiatopic peptides and antithrombotic peptides, but is not limited thereto.

The functional peptide may be added between the C-terminus, the N-terminus, or both of the mussel adhesive protein or hybrid mussel adhesive protein by genetic recombination technology. For example, in the case of the fusion protein FP-151 having a structure in which FP-1 is fused to both ends of FP-5, an antibacterial peptide may be added between FP-1 and FP-5. In addition, different antibacterial peptides may be added between both ends or the fusion protein. For example, the antibacterial peptide may be an α-helical 23 amino acid peptide isolated from the skin of the African frog Xenopus laevis, an antibacterial peptide such as Magainin or Dermaseptin, or human defen Antibacterial peptides such as human defensin, cathelicidin LL-37, and histatin may be used, but are not limited thereto.

In the present invention, in the case of the antibacterial peptide fused to the adhesion protein, any peptide derived from nature or artificially synthesized may be used without limitation. Antibacterial peptides exert an antibacterial effect through a mechanism that destroys the cell membrane of microorganisms or penetrates the cell membrane and inhibits metabolic function. In the present invention, any antibacterial peptide that exerts an antibacterial effect as a mechanism of destroying cell membranes of microorganisms can be used without limitation. Preferably, the antimicrobial peptide fused to the adhesion protein may be selected from antimicrobial peptides that are effective against Gram-positive bacteria as well as Gram-negative bacteria. More preferably, KLWKKWAKKWLKLWKA (SEQ ID NO: 20), FALALKALKKL (SEQ ID NO: 21), ILRWPWWPWRRK (SEQ ID NO: 22), AKRHHGYKRKFH (SEQ ID NO: 23), KWKLFKKIGAVLKVL (SEQ ID NO: 24), IWSILAPLG (SEQ ID NO: 24), LVKLVAGIKKKFLKAGW No. 26), GIGAVLKVLTTGLPALISWI (SEQ ID NO: 27), SWLSKTAKKGAVLKVL (SEQ ID NO: 28), KKLFKKILKYL (SEQ ID NO: 29), GLKKLISWIKRAAQQG (SEQ ID NO: 30), or an antibacterial peptide of GWLKKIGKKIERVGQHTRDATIQGLGIAQ (SEQ ID NO: 31) (SEQ ID NO: 31), but limited thereto it is not

As another physiologically functional adhesive provided in the present invention, a peptide having an antiviral or anticancer effect may be used. In the case of the anticancer adhesive, it may include, without limitation, any peptide present in nature or artificially synthesized as a peptide having an anticancer effect. Preferably, the antiviral peptide is RRWWCRC (SEQ ID NO: 32), the anti-cancer peptide is THRPPMWSPVWP (SEQ ID NO: 33), KLLLKLLKKLLKLLKKK (SEQ ID NO: 34), FLKLLKKLAAKLF (SEQ ID NO: 35), RLLRRLLRRLLRRLLRRLLR (SEQ ID NO: 36), or KLAKLAKKLAKLLRRLLR (SEQ ID NO: 36), or (SEQ ID NO: 37), but is not limited thereto.

In the present invention, in order to provide an antimicrobial adhesive protein having a broad spectrum of antimicrobial effects, a coating composition based on an antimicrobial adhesive protein in which different antimicrobial peptides are added to the C-terminus and the N-terminus of the adhesive protein may be provided. According to a preferred embodiment of the present invention, the antimicrobial coating composition is a peptide FALALKALKKL (SEQ ID NO: 21) that is effective against gram-negative bacteria is added to the C-terminus, and the peptide AKRHHGYKRKFH (SEQ ID NO: 23) that is effective against gram-positive bacteria is added to the N-terminus. ) to which an antibacterial adhesive protein has been added may be used.

In the present invention, in the mussel adhesion protein to which the antibacterial peptide is fused, the tyrosine residue among the constituent amino acids can be changed to DOPA and further to dopaquinone through chemical modification, and the modified dopa and dopaquinone are used in adhesion to the surface. It can play a very important role. According to one embodiment of the present invention, chemical modification of the recombinant mussel adhesive protein can be performed using a mushroom-derived tyrosinase enzyme that can mediate such chemical modification. The chemically modified antibacterial mussel adhesive protein can be attached to various materials such as metal, plastic, and glass without limitation.

The concentration of the coating composition based on the antimicrobial adhesion protein can be adjusted according to the concentration of the added antimicrobial peptide and the introduced acrylate. Preferably, the concentration of the antimicrobial coating composition is 0.1 to 1% (wt/wt), more preferably 0.1 to 0.3% (wt/wt).

The acrylate-based antimicrobial coating composition introduced into the antimicrobial adhesive protein of the present invention is a UV photocurable coating agent. As a photoinitiator, benzoyl peroxide, Irgacure 184, etc. may be used, but is not limited thereto. The weight ratio of the acrylate and the antimicrobial adhesive protein is 1:0.01, preferably 1:0.001.

All of the acrylates used in the present invention may be basically incorporated into the molecular backbone of the adhesion protein. The antimicrobial coating composition provided in the present invention is composed of an antimicrobial adhesive protein into which one or more acrylates selected from the group consisting of glycidyl acrylate, urethane acrylate, polyester acrylate and epoxy acrylate are introduced.

In addition, the present invention provides a physiologically functional adhesive composition comprising the physiologically functional adhesive protein.

In addition, the UV photocurable antibacterial coating composition of the present invention provides an antibacterial functional film comprising an antibacterial adhesive protein.

The film used to prepare the antibacterial film coated with the antibacterial composition may be a polyethylene or polypropylene film commonly used for food packaging, smartphone screen protection, etc., but is not limited thereto. The amount of the UV photocurable antimicrobial composition to be applied may be appropriately selected in consideration of the amount of the antibacterial adhesive protein, the type of the coating target, and the like.

In one embodiment of the present invention, urethane acrylate containing an antibacterial adhesive protein was applied using a polystyrene film and then photocured to prepare an antibacterial coating film. The antibacterial coating film confirmed the reduction rate of bacteria on the uncoated surface and the coated surface for E. coli, a gram-negative bacteria (see FIG. 3).

The photocurable antibacterial coating composition of the present invention mixed with antibacterial adhesive protein alone or acrylate is coated on the surface of a mobile phone liquid crystal protective film, food packaging material, medical device, etc. to ensure stability against harmful microorganisms. In particular, according to the present invention, antibacterial activity is continuously maintained based on the strong adhesion of mussel adhesive protein, thereby preventing a decrease in antimicrobial activity due to dissolution of antibacterial substances.

The above-described and further features and advantages of the present invention will become apparent when considered in conjunction with the drawings and the following embodiments, which are provided for illustrative purposes.
1 shows a flow chart for introducing an acrylate into a mussel adhesion protein.
2 shows the results of NMR analysis of the acrylated mussel adhesive protein. As a result of NMR analysis of the mussel adhesive protein and the acrylated mussel adhesive protein, a hydrogen peak of acrylate was confirmed, indicating that an acrylate group was introduced into the molecular backbone of the mussel adhesive protein by the acrylate process of FIG. 1 .
Figure 3 shows the antibacterial activity against Staphylococcus aureus after coating the acrylated adhesive protein containing the antibacterial peptide B on the polyester fabric. Staphylococcus aureus was further reduced by about 15% in the fabric (SA-A) coated with the antibacterial adhesive compared to the control (SA-C) coated with the general mussel adhesive.

The following examples are provided to illustrate preferred embodiments of the present invention, and the present invention is not limited in scope by the following specific embodiments, which are provided for illustrative purposes only. It is apparent that functionally equivalent products, compositions, and methods as disclosed herein may be included within the scope of the present invention.

Preparation of expression vector of antibacterial peptide fusion mussel adhesive protein

For the production of antibacterial peptide fusion mussel adhesive protein, a genetic sequence in which a conventional antibacterial peptide sequence is added to the C-terminal or N-terminal region of the mussel adhesive protein was designed and an expression vector was commissioned to Novacell Technology. The constructed vector was transformed into E. coli BL21 (DE3), and the added sequence is shown in Table 1.

Preparation of Antibacterial Peptide-Fused Mussel Adhesive Proteins

2-1. E. coli BL21 (DE3) culture

E. coli BL21(DE3) was cultured in LB (5 g/ℓ yeast extract, 10 g/ℓ Tryptone and 10 g/ℓ NaCl) medium, and when the absorbance of the culture medium reached about 0.6 at 600 nm, the final concentration of IPTG was Expression of recombinant antimicrobial peptide fusion mussel adhesion protein was induced by addition at 1 mM. The E. coli BL21 (DE3) culture medium was centrifuged at 13,000 rpm and 4°C for 10 minutes to obtain a cell pellet, which was stored at -80°C.

2-2. Confirmation of expression of antibacterial peptide fusion mussel adhesive protein

The cell pellet is diluted in 100 μg of buffer for SDS-PAGE (0.5 M Tris-HCl, pH 6.8, 10% glycerol, 5% SDS, 5% β-mercaptoethanol, 0.25% bromophenol blue), boiled at 100°C for 5 minutes, and denatured. did it In the case of SDS-PAGE, the sample was electrophoresed on 15% SDS-polyacrylamide gel, and protein bands were detected and confirmed using Coomasie blue staining.

2-3. Purification of Antibacterial Peptide-Fused Mussel Adhesive Proteins

The cell pellet obtained in Example 2-1 was stirred using a lysis buffer (2.4 g / ℓ sodium phosphate monobasic, 5.6 g / ℓ sodium phosphate dibasic, 10 mM EDTA and 1% Triton X-100), and , cells were disrupted using a high-pressure disrupter. The lysate was centrifuged at 9,000 rpm for 20 minutes to obtain an insoluble protein aggregate including mussel adhesive protein. The antibacterial peptide fusion mussel adhesive protein was extracted from the insoluble protein aggregate using 25% acetic acid, and the supernatant containing the mussel protein was recovered by centrifugation at 9,000 rpm for 20 minutes. The recovered supernatant was raised to pH 12.8 using 10 N NaOH, and centrifuged under the same conditions to recover the supernatant. The supernatant was neutralized to pH 6-7 using acetic acid and then centrifuged under the same conditions to obtain a precipitate of antibacterial peptide fusion mussel adhesive protein. The obtained precipitate was dissolved in an appropriate amount of purified water and then lyophilized to obtain a lyophilized product of antibacterial peptide fusion mussel adhesive protein with a purity of 90% or more.

Acrylation of antibacterial adhesives

Prepare 10 ml of an acidic solution adjusted to pH 4.0 by adding hydrochloric acid to distilled water, and 10 mg of the antibacterial adhesive MAPTrix™ obtained in Example 2 and 10 mg of glycidyl acrylate in each 1 ml solution was completely dissolved to prepare a stock solution. A 0.2 wt% antibacterial adhesive MAPTrix™ solution was prepared by mixing 3.875 ml of sodium phosphate buffer and 1 ml of MAPTrix™ solution (1 wt%) in a 10 ml vial. To a 0.2 wt% MAPTrix™ solution, 0.125 ml of glycidyl acrylate (1 wt% solution) was added so that the acrylate/lysine molar ratio was 0.1. The temperature of the reaction mussel was heated to 50° C. and acrylated for 8 hours. When the reaction was completed, dialyzed at 4° C. using a UF membrane having a molecular weight cut-off of 13 kDa, exchanged every 8 hours, a total of 4 times. After dialysis, the presence and extent of acrylated solution was measured through NMR or spectroscopic analysis.

Determination of antibacterial activity of antibacterial adhesives

A coating solution was prepared in order to measure the antimicrobial activity of the antimicrobial adhesive protein obtained in Example 3. The antibacterial coating agent was prepared by using distilled water at a concentration of 10 to 0.01 mg/ml of an acrylated antibacterial adhesive. This antibacterial coating solution was sprayed onto the polyester fabric and coated, and then the fabric surface was coated for 1 hour. Thereafter, the surface was washed three times with sterile PBS, and then dried again for 24 hours. When the surface is completely dry, dilute the pre-cultured Staphylococcus aureus test solution with PBS to 10 ⁴ CFU/ml, make 10 pieces of antibacterial fiber fabric 0.5 cm × 0.5 cm, and put it in a tube containing Staphylococcus aureus. stirred for hours. As a result, it was found that the antibacterial coated textile fabric had a more improved antibacterial effect by reducing staphylococci by about 15% compared to the control (FIG. 3).

Coating Composition of Acrylated Antimicrobial Adhesive Protein

An antibacterial film was prepared by exposing the acrylated antibacterial adhesive to two UV bulbs in a UV room (wavelength 285 nm) heated to 90° C. and curing it for 10 minutes. The antibacterial activity test of the prepared antibacterial film was performed on E. coli, staphylococcus, pneumococcus, and candida according to the same method and procedure as in Example 4. As a result, compared with the uncoated control group, growth of major host bacteria such as E. coli, Staphylococcus aureus, Pneumonia, and Candida on the surface of the film coated with the acrylated antibacterial adhesive was not observed.

<110> LEE, SANG JAE <120> Biofunctional Adhesive Composition <130> 0001 <160> 37 <170> KopatentIn 2.0 <210> 1 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> model peptide of the tandem repeat decapeptide derived from foot protein 1 (FP-1, Mytilus edulis) <400> 1 Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys 1 5 10 <210> 2 <211> 20 <212> PRT <213 > Artificial Sequence <220> <223> 2 times repeated sequence derived from foot protein 1 (FP-1, Mytilus edulis) <400> 2 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> 3 <211> 60 <212> PRT <213> Artificial Sequence <220> <223> 6 times repeated sequence derived from foot protein 1 (FP-1, Mytilus edulis) <400> 3 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 T yr Pro Pro Thr Tyr Lys 50 55 60 <210> 4 <211> 39 <212> PRT <213> Artificial Sequence <220> <223> partial sequence of foot protein type 2 (FP-2, Mytilus californianus) <400> 4 Glu Val His Ala Cys Lys Pro Asn Pro Cys Lys Asn Asn Gly Arg Cys 1 5 10 15 Tyr Pro Asp Gly Lys Thr Gly Tyr Lys Cys Lys Cys Val Gly Gly Tyr 20 25 30 Ser Gly Pro Thr Cys Ala Cys 35 <210 > 5 <211> 52 <212> PRT <213> Artificial Sequence <220> <223> Foot protein type 3 (FP-3, Mytilus edulis) <400> 5 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> 6 <211> 46 <212> PRT <213> Artificial Sequence <220> <223> Foot protein type 3 (FP-3, Mytilus galloprovincialis : mgfp-3A) <400> 6 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> 7 <211> 50 <212> PRT <213> Artificial Sequence <220> <223> Foot protein type 3 (FP-3, Mytilus edulis: mefp-3F) <400> 7 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> 8 <211> 44 <212> PRT <213> Artificial Sequence <220> <223> Foot protein type 3 (FP-3, Mytilus californianus) <400> 8 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> 9 <211> 60 <212> PRT <213> Artificial Sequence <220> <223> partial sequence from foot protein type 4 (Mytilus californianus) <400> 9 Gly His Val His Arg His Arg Val Leu His Lys His Val Hi s Asn His 1 5 10 15 Arg Val Leu His Lys His Leu His Lys His Gln Val Leu His Gly His 20 25 30 Val His Arg His Gln Val Leu His Lys His Val His Asn His Arg Val 35 40 45 Leu His Lys His Leu His Lys His Gln Val Leu His 50 55 60 <210> 10 <211> 75 <212> PRT <213> Artificial Sequence <220> <223> Foot protein type5 (FP-5, Mytilus edulis) <400> 10 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> 11 <211> 76 <212> PRT <213> Artificial Sequence <220> <223> Foot protein 5 (FP-5, Mytilus edulis) <400> 11 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> 12 <211> 71 <212> PRT <213> Artificial Sequence <220> <223> Foot protein 5 (FP-5, Mytilus coruscus) <400> 12 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> 13 <211> 76 <212> PRT <213> Artificial Sequence <220> <223> mussel adhesive protein foot protein type5 from (Mytilus galloprovincialis) <400> 13 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 T yr 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> 14 <211> 99 <212> PRT <213> Artificial Sequence <220> <223> mussel adhesive protein foot protein type 6 <400> 14 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> 15 <211> 194 <212> PRT <213> Artificial Sequence <220> <223> hybrid mussel adhesive protein (FP-151, MEFP-5 based) <400> 15 Ala Lys Pro Ser Tyr Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro 1 5 10 15 Pro Thr Tyr Lys Ala Lys Pro Ser T yr 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 Ser Ser Glu Glu 50 55 60 Tyr Lys Gly Gly Tyr Tyr Pro Gly Asn Ala Tyr His Tyr His Ser Gly 65 70 75 80 Gly Ser Tyr His Gly Ser Gly Tyr His Gly Gly Tyr Lys Gly Lys Tyr 85 90 95 Tyr Gly Lys Ala Lys Lys Tyr Tyr Tyr Lys Tyr Lys Asn Ser Gly Lys 100 105 110 Tyr Lys Tyr Leu Lys Lys Ala Arg Lys Tyr His Arg Lys Gly Tyr Lys 115 120 125 Tyr Tyr Gly Gly Ser Ser Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys 130 135 140 Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro 145 150 155 160 Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys 165 170 175 Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr 180 185 1 90 Tyr Lys <210> 16 <211> 196 <212> PRT <213> Artificial Sequence <220> <223> hybrid mussel adhesive protein (FP-151, MGFP-5 based) <400> 16 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 Thr 35 40 45 Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ser Ser Glu Glu 50 55 60 Tyr Lys Gly Gly Tyr Tyr Pro Gly Asn Thr Tyr His Tyr His Ser Gly 65 70 75 80 Gly Ser Tyr His Gly Ser Gly Tyr His Gly Gly Tyr Lys Gly Lys Tyr 85 90 95 Tyr Gly Lys Ala Lys Lys Tyr Tyr Tyr Lys Tyr Lys Asn Ser Gly Lys 100 105 110 Tyr Lys Tyr Leu Lys Lys Ala Arg Lys Tyr His Arg Lys Gly Tyr Lys 115 120 125 Lys Tyr Tyr Gly Gly Gly Ser Ser Ala Lys Pro Ser Tyr Pro Pro Thr 130 135 140 Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser 145 150 155 160 Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys 165 170 175 Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro 180 185 190 Pro Thr Tyr Lys 195 <210> 17 <211> 192 <212> PRT <213> Artificial Sequence <220> <223> hybrid mussel adhesive protein (FP-151, MCFP-5 based) <400> 17 Ala Lys Pro Ser Tyr 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 Tyr Asp Gly Tyr 50 55 60 Ser Asp Gly Tyr Tyr Pro Gly Ser Ala Tyr Asn Tyr Pro Ser Gly Ser 65 70 75 80 His Gly Tyr His Gly His Gly Tyr Lys Gly Lys Tyr Tyr Gly Lys Gly 85 90 95 Lys Lys Tyr Tyr Tyr Lys Tyr Lys Arg Thr Gly Lys Tyr Lys Tyr Leu 100 105 110 Lys Lys Ala Arg Lys T yr His Arg Lys Gly Tyr Lys Lys Tyr Tyr Gly 115 120 125 Gly Gly Ser Ser Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys 130 135 140 Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Thr 145 150 155 160 Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser 165 170 175 Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys 180 185 190 <210> 18 <211> 177 < 212> PRT <213> Artificial Sequence <220> <223> hybrid mussel adhesive protein (FP-131) <400> 18 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 Gly Cys Arg Ala 50 55 60 Asp Tyr Tyr Gly Pro Lys Tyr Gly Pro Pr o Arg Arg Tyr Gly Gly Gly 65 70 75 80 Asn Tyr Asn Arg Tyr Gly Gly Ser Arg Arg Tyr Gly Gly Tyr Lys Gly 85 90 95 Trp Asn Asn Gly Trp Lys Arg Gly Arg Trp Gly Arg Lys Tyr Tyr Glu 100 105 110 Phe Glu Phe Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro 115 120 125 Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr 130 135 140 Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr 145 150 155 160 Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Lys 165 170 175 Leu <210> 19 <211> 180 <212> PRT <213> Artificial Sequence <220> <223> hybrid mussel adhesive protein (FP-251) <400> 19 Met Glu Val His Ala Cys Lys Pro Asn Pro Cys Lys Asn Asn Gly Arg 1 5 10 15 Cys Tyr Pro Asp Gly Lys Thr Gly Tyr Lys Cys Lys Cys Val Gly Gly 20 25 30 Tyr Ser Gly Pro Thr Cys Ala Cys Ser Ser Glu Glu Tyr Lys Gly Gly 35 40 45 Tyr Tyr Pro Gly Asn Ser Asn His Tyr His Ser Gly Gly Ser Tyr His 50 55 60 Gly Ser Gly Tyr His Gly Gly Tyr Lys Gly Lys Tyr Tyr Gly Lys Ala 65 70 75 80 Lys Lys Tyr Tyr Tyr Lys Tyr Lys Asn Ser Gly Lys Tyr Lys Tyr Leu 85 90 95 Lys Lys Ala Arg Lys Tyr His Arg Lys Gly Tyr Lys Lys Tyr Tyr Gly 100 105 110 Gly Ser Ser Glu Phe Glu Phe Ala Lys Pro Ser Tyr Pro Pro Thr Tyr 115 120 125 Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr 130 135 140 Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala 145 150 155 160 Lys Pro Ser Tyr Pro Pro Thr Tyr Lys Ala Lys Pro Ser Tyr Pro Pro 165 170 175 Thr Tyr Lys Lys 180 <210> 20 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (KLWKKWAKKWLKLWKA) <400> 20 Lys Leu Trp Lys Lys Trp Ala Lys Lys Trp Leu Lys Leu Trp Lys Ala 1 5 10 15 <210> 21 <211> 11 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (FALALKALKKL) <400> 21 Phe Ala Leu Ala Leu Lys Ala Leu Lys Lys Leu 1 5 10 <210> 22 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (ILRWPWWPWRRK) <400> 22 Ile Leu Arg Trp Pro Trp Trp Pro Trp Arg Arg Lys 1 5 10 <210> 23 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (AKRHHGYKRKFH) <400> 23 Ala Lys Arg His His Gly Tyr Lys Arg Lys Phe His 1 5 10 <210> 24 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (KWKLFKKIGAVLKVL) <400> 24 Lys Trp Lys Leu Phe Lys Lys Ile Gly Ala Val Leu Lys Val Leu 1 5 10 15 <210> 25 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (LVKLVAGIKKFLKWK) <400> 25 Leu Val Lys Leu Val Ala Gly Ile Lys Lys Phe Leu Lys Trp Lys 1 5 10 15 <210> 26 <211> 25 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (IWSILAPLGTTLVKLVAGIGQQKRK) <400> 26 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> 27 <211> 20 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (GIGAVLKVLTGLPALISWI) <400> 27 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> 28 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Anti- microbacterial peptide (SWLSKTAKKGAVLKVL) <400> 28 Ser Trp Leu Ser Lys Thr Ala Lys Lys Gly Ala Val Leu Lys Val Leu 1 5 10 15 <210> 29 <211> 11 <212> PRT <213> Artificial Sequence <220> < 223> Anti-microbacterial peptide (KKLFKKILKYL) <400> 29 Lys Lys Leu Phe Lys Lys Ile Leu Lys Tyr Leu 1 5 10 <210> 30 <211> 16 <212> PRT <213> Artificial Sequence <220> <223> Anti-microbacterial peptide (GLKKLISWIKRAAQQG ) <400> 30 Gly Leu Lys Lys Leu Ile Ser Trp Ile Lys Arg Ala Ala Gln Gln Gly 1 5 10 15 <210> 31 <211> 39 <212> PRT <213> Artificial Sequence <220> <223> Anti- microbacterial peptide (GWLKKIGKKIERVGQHTRDATIQGLGIAQQAANVAATAR) <400> 31 Gly Trp Leu Lys Lys Ile Gly Lys Lys Ile Glu Arg Val Gly Gln His 1 5 10 15 Thr Arg Asp Ala 30 Asn A Val Gln 25 Gly Leu Gly Ile Ala Gln Gln A Ala Ala Thr Ala Arg 35 <210> 32 <211> 7 <212> PRT <213> Artificial Sequence <220> <223> Anti-viral peptide (RRWWCRC) <400> 32 Arg Arg Trp Trp Cys Arg Cys 1 5 < 210> 33 <211> 12 <212> PRT <213> Artificial Sequence <220> <223> Anti-cancer peptide (THRPPMWSPVWP) <400> 33 Thr His Arg Pro Pro Met Trp Ser Pro Val Trp Pro 1 5 10 <210 > 34 <211> 17 <212> PRT <213> Artificial Sequence <220> <223> Anti-cancer peptide (KLLLKLLKKLLKLLKKK) <400> 34 Lys Leu Leu Leu Lys Leu Leu Lys Lys Leu Leu Lys Leu Leu Lys Lys 1 5 10 15 Lys <210> 35 <211> 13 <212> PRT < 213> Artificial Sequence <220> <223> Anti-cancer peptide (FLKLLKKLAAKLF) <400> 35 Phe Leu Lys Leu Leu Lys Lys Leu Ala Ala Lys Leu Phe 1 5 10 <210> 36 <211> 20 <212> PRT < 213> Artificial Sequence <220> <223> Anti-cancer peptide (RLLRRLLRRLLRRLLRRLLR) <400> 36 Arg Leu Leu Arg Arg Leu Leu Arg Arg Leu Leu Arg Arg Leu Leu Arg 1 5 10 15 Arg Leu Leu Arg 20 <210> 37 <211> 14 <212> PRT <213> Artificial Sequence <220> <223> Anti-cancer peptide (KLAKLAKKLAKLAK)<400> 37 Lys Leu Ala Lys Leu Ala Lys Lys Leu Ala Lys Leu Ala Lys 1 5 10

Claims (11)

A physiologically functional adhesive protein in which a physiologically functional peptide is bound to the C-terminus or N-terminus of the acrylate-attached adhesive protein. The method according to claim 1,
The adhesion protein is a physiologically functional adhesion protein, which is a mussel-derived adhesion protein. 3. The method according to claim 2,
The mussel-derived adhesive protein is a group consisting of FP-1 having an amino acid sequence selected from the group consisting of SEQ ID NOs: 1 to 3, FP-2 having an amino acid sequence of SEQ ID NO: 4, and SEQ ID NOs: 5 to SEQ ID NO: 8 FP-3 having an amino acid sequence selected from, FP-4 having an amino acid sequence of SEQ ID NO: 9, FP-5 having an amino acid sequence selected from the group consisting of SEQ ID NO: 10 to SEQ ID NO: 13, described in SEQ ID NO: 14 FP-6 having an amino acid sequence, FP-151 having an amino acid sequence selected from the group consisting of SEQ ID NO: 15 to SEQ ID NO: 17, FP-131 having an amino acid sequence consisting of SEQ ID NO: 18, and having an amino acid sequence of SEQ ID NO: 19 A physiologically functional adhesive protein selected from the group consisting of FP-251 and fragments of each protein. The method according to claim 1,
The physiologically functional peptide is a physiologically functional adhesive protein having a function of destroying the cell membrane by acting on the cell membrane. 5. The method according to claim 4,
The physiologically functional peptide is a physiologically functional adhesive protein selected from the group consisting of an antibacterial peptide, an antiviral peptide, an anticancer peptide, an antiatopic peptide and an antithrombotic peptide. 6. The method of claim 5,
The physiologically functional peptide is a physiologically functional adhesive protein selected from the group consisting of an antibacterial peptide, an antiviral peptide and an anticancer peptide. 7. The method of claim 6,
The antibacterial peptide is a physiologically functional adhesive protein having an amino acid sequence selected from the group consisting of SEQ ID NO: 20 to SEQ ID NO: 31. 7. The method of claim 6,
The antiviral peptide is a physiologically functional adhesive protein having the amino acid sequence of SEQ ID NO: 32. 7. The method of claim 6,
The anticancer peptide is a physiologically functional adhesive protein having an amino acid sequence selected from the group consisting of SEQ ID NOs: 33 to 37. The method according to claim 1,
The acrylate is a physiologically functional adhesive protein selected from the group consisting of glycidyl acrylate, urethane acrylate, polyester acrylate and epoxy acrylate. A physiologically functional adhesive composition comprising the physiologically functional adhesive protein according to any one of claims 1 to 10.

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