KR20200071416A - Poecilocorisin-1 peptide isolated from Poecilocoris lewisi or antimicrobial, antimycotic and antiinflammatory composition comprising it - Google Patents

Abstract

The present invention relates to poecilocorisin-1 peptide derived from Poecilocoris lewisi and an antimicrobial, antimycotic or anti-inflammatory composition comprising the poecilocorisin-1 peptide as an effective component. The poecilocorisin-1 peptide according to the present invention, has excellent antimicrobial or antimycotic effects against Staphylococcus aureus, Escherichia coli O157, Candida albicans, and the like, is capable of inhibiting secretion of nitric oxide (NO), and is capable of suppressing the expression of IL-6, iNOS, COX-2, and the like, thereby being easily usable as a therapeutic agent for various inflammatory diseases.

Description

Poesilocorisin-1 peptide isolated from Poecilocorisin-1 peptide isolated from Poecilocoris lewisi or antimicrobial, antimycotic and antiinflammatory composition comprising it as an active ingredient

The present invention relates to a composition for antimicrobial, antifungal, or anti-inflammatory, comprising a poesilochoricin-1 peptide derived from a vast stink bug, as an active ingredient.

Insects have evolved toward adapting to the environment in which they live and securing their own special physiological control mechanisms and substances. Recently, research on the development of new drug candidates using bioactive substances of insects has been actively conducted [ Insect Biochem . Mol. Biol. 41, 747-769]. As one of the candidates for insects, there is a clown stink bug ( Poecilocoris lewisi ), but currently, little is known about the method of applying the pharmacological mechanism or pharmaceutical composition using the clapper .

On the other hand, some of the substances that play an important role in the process for maintaining homeostasis of organisms are bioactive substances derived from various organisms. Numerous studies have been conducted on a number of bioactive substances, and among them, antibacterial peptides isolated from various organisms are known to act in various ways, including bacteria, fungi, and viruses. In addition, antimicrobial peptides are known to play an important role in host defense and innate immune systems.

Infection with pathogenic microorganisms is one of the most common and fatal causes of human disease, but unfortunately, the abuse of antibiotics has caused antibiotic resistance of pathogenic microorganisms. Indeed, the rate at which pathogenic microorganisms are resistant to new antibiotics is much faster than the rate at which analogs of new antibiotics are developed. For example, pathogenic microbial species, such as Enterococcus faecalis , Mycobacterium tuberculosis , and Pseudomonas aeruginosa , which are potentially life-threatening, are known to date. It has developed resistance to all antibiotics. Tolerance of antibiotics is a phenomenon distinct from resistance to antibiotics, which was first discovered in Pneumococcus sp. in the 1970s and provided important clues to the mechanism of action of penicillin. Resistant species stop growing in the presence of conventional concentrations of antibiotics, but do not die as a result. This resistance occurs because the activity of bacterial autolytic enzymes, such as autolysin, does not occur when antibiotics inhibit cell wall synthase, which causes penicillin to produce endogenous hydrolytic enzymes. By activating it, it kills bacteria and bacteria also inhibit their activity, resulting in survival even in antibiotic treatment. It is clinically important for pathogenic microorganisms to be resistant to antibiotics, because when it becomes impossible to eradicate resistant microorganisms, the effectiveness of antibiotic treatment in clinical infections decreases. In addition, resistance is considered to be a prerequisite for resistance to antibiotics, because it produces strains that survive antibiotic treatment. These strains acquire new genetic elements that are resistant to antibiotics and continue to grow even in the presence of antibiotics. Since it is known that the pathogenic microorganisms exhibiting practically all resistance are also resistant, the development of new antibiotics capable of killing the pathogenic microorganisms having such antibiotic resistance is urgent.

Inflammation is one of the biological tissue's defense responses to a certain stimulus, and refers to a complex lesion that combines tissue degeneration, circulatory disorder and exudation, and tissue proliferation. The causes are mechanical injuries, physical factors such as temperature and radiation, chemical factors such as poisons, and parasitic organisms such as bacterial infections. In addition to these main causes, its occurrence is complicated by several minor factors and the predisposition or immunity of the individual. In addition, the inflammatory reaction can be said to be one of the most important pathological mechanisms according to the host's defense mechanism against wounds, microbial infections, and the like. Macrophages are the most representative immune cells that regulate this inflammatory response, and activated macrophages are TNF-α (tumor necrosis factor-α), IL-6 (interleukin-6), PGE2 (prostaglandin E2), NO (nitric oxide) ), ROS (reactive oxygen species) and various inflammatory mediators. On the other hand, overexpression of these inflammatory mediators induces rheumatoid arthritis, osteoporosis, sepsis, vascular disease, cancer, etc. (Lawrence, T. et al., 2012).

Accordingly, the present inventors were able to complete the present invention by studying the various physiological activities using a peptide derived from a clown nori, while confirming that the novel peptide poesilochoricin-1 has antibacterial, antifungal or anti-inflammatory effects. .

Korean Registered Patent No. 10-1660381 (Invention name: Insect N-glycan and its use, Applicant: Korea) Korean Patent Publication No. 10-2011-0013074 (Name of invention: New use and manufacturing method of insect glycosaminoglycan, Applicant: Korea)

Lawrence, T. et al., Anti-inflammatory lipid mediators and insights into the resolution of inflammation., Nat. Rev. Immunol., 2002, 2, 787-795.

An object of the present invention is to provide a composition for antibacterial, antifungal, or anti-inflammatory, comprising a poesilochoricin-1 peptide derived from a vast stink bug, as an active ingredient.

The present invention relates to an antimicrobial, antifungal or anti-inflammatory peptide, characterized in that it consists of the amino acid sequence of SEQ ID NO: 1, derived from the clown stink bug ( Poecilocoris lewisi ).

SEQ ID NO: KKRKKKAFALKFVVDLI-NH ₂

The peptide may exhibit antibacterial activity against any one or more of Staphylococcus aureus and Escherichia coli 0-157, and antifungal activity against Candida albicans Can represent

Due to the antibacterial and antifungal effects, the present invention can also provide an antibiotic, food preservative, cosmetic preservative or pharmaceutical preservative containing the peptide as an active ingredient.

Accordingly, the present invention provides an antibacterial and antifungal anti-inflammatory composition comprising the peptide as an active ingredient, and provides a composition for preventing or treating inflammatory diseases comprising the peptide. The inflammatory diseases include inflammatory bowel disease, inflammatory collagen vascular disease, glomerulonephritis, inflammatory skin disease, sarcoidosis, retinitis, gastritis, hepatitis, enteritis, arthritis, tonsillitis, sore throat, bronchitis, pneumonia, pancreatitis, sepsis, cystitis, nephritis and neuritis. It can be selected from the group consisting of.

Hereinafter, the present invention will be described in detail.

The present invention relates to a peptide represented by SEQ ID NO: 1 synthesized from the gene of an antibacterial, antifungal or anti-inflammatory peptide isolated from a vast stink bug. Therefore, the present invention may be directed to an antibacterial, antifungal or anti-inflammatory peptide isolated directly from a vast stink bug having the same sequence as SEQ ID NO: 1.

In addition, the present invention may be directed to an anti-inflammatory peptide isolated directly from a vast stink bug having the same sequence as SEQ ID NO: 1.

The peptide of the present invention may have a carboxyl terminus of -NH ₂ form or -OH form.

In the present invention, in order to identify the peptide gene derived from the clown stink bug ( Poecilocoris lewisi ), first, the clown stink streak is rapidly frozen with liquid nitrogen to separate the entire RNA, and this is the genetic information about the transcripts in the clown stink bug using RNA seq analysis. It is confirmed, and based on the sequence of the amino acid (peptide) translated from each transcript, it is possible to select unigene, which is presumed to be a peptide exhibiting anti-inflammatory activity, by using the properties of an existing anti-inflammatory peptide.

The amino acid sequence of the peptide is KKRKKKAFALKFVVDLI-NH ₂ , which is composed of 17 amino acids, and is named Poecilocorisin-1.

The present invention may provide a composition for preventing or treating an inflammatory disease containing the peptide, wherein the inflammatory disease is inflammatory bowel disease, inflammatory collagen vascular disease, glomerulonephritis, inflammatory skin disease, sarcoidosis, retinitis, gastritis, hepatitis, It may be selected from the group consisting of enteritis, arthritis, tonsillitis, sore throat, bronchitis, pneumonia, pancreatitis, sepsis, cystitis, nephritis and neuritis.

In addition, the present invention provides various pharmaceutical compositions comprising the peptide as an active ingredient. The pharmaceutical composition may be an anti-inflammatory composition, a pharmaceutical composition for preventing or treating inflammatory diseases.

The pharmaceutical composition of the present invention can be administered to various mammals, such as rats, livestock, and humans. All modes of administration can be expected, for example, by oral, rectal or intravenous, intramuscular, subcutaneous, intrauterine dura mater or intracranial injection.

The pharmaceutical composition containing the poesilochoricin-1 peptide of the present invention can also be administered parenterally during clinical administration and can be used in the form of general pharmaceutical preparations. The peptide or a composition containing the same may actually be administered in various parenteral formulations. When formulated, it is usually prepared using diluents or excipients such as fillers, extenders, binders, wetting agents, disintegrants, surfactants, etc. Can be. Formulations for parenteral administration may include sterile aqueous solutions, non-aqueous solvents, suspensions, emulsions, lyophilized preparations, and suppositories. As the non-aqueous solvent and suspension solvent, propylene glycol, polyethylene glycol, vegetable oil such as olive oil, and injectable ester such as ethyl oleate may be used. As a base for suppositories, witepsol, macrogol, tween 61, cacao butter, laurin butter, and glycerogelatin may be used.

In addition, the poesilochoricin-1 peptide of the present invention can be used in combination with various carriers allowed as medicaments such as physiological saline or organic solvents, and glucose, sucrose, or dex to increase stability or absorption. Carbohydrates such as tran, antioxidants such as ascorbic acid or glutathione, chelating agents, low molecular weight proteins or other stabilizers can be used as medicaments.

In the pharmaceutical composition, the total effective amount of the poesilochoricin-1 peptide of the present invention or a peptide having 95% or more homology thereto is a single dose by bolus form or infusion for a relatively short period of time ( It can be administered to a patient as a single dose, and can be administered by a fractionated treatment protocol in which multiple doses are administered for a long time. Considering this, the concentration is determined by taking into consideration various factors such as the patient's age and health status, as well as the administration route and number of treatments of the pharmaceutical composition. Appropriate effective dosages for specific uses as pharmaceutical compositions containing the novel peptides of the invention may be determined.

The present invention relates to a composition for antimicrobial, antifungal, or anti-inflammatory, comprising a poesilochoricin-1 peptide derived from a vast stink bug, as an active ingredient. The poesilochoricin-1 peptide of the present invention has an antibacterial or antifungal effect against Staphylococcus aureus , Escherichia coli 0-157, Candida albicans , etc. Excellent, it has the effect of inhibiting NO secretion and suppressing the expression of IL-6, iNOS, COX-2, etc., and thus can be easily used as a therapeutic agent for various inflammatory diseases.

As a prior art for the present invention, the pharmacological use of glycosaminoglycan separated from a slag material is disclosed in Korean Patent Registration No. 10-1660381 and Korean Patent Publication No. 10-2011-0013074. It has never been disclosed that a peptide composition derived from clown stink bugs has a similar function, and further, in the peptide technology related to clapper stink bugs, a peptide having the same amino acid sequence as the present invention has antibacterial, antifungal or anti-inflammatory effects. It has not been done yet.

1 is a graph showing antibacterial activity against Escherichia coli and Staphylococcus aureus , and antifungal activity against Candida albicans .
Figure 2 is a graph showing the cytotoxicity of the poesilocolysine-1 peptide against mouse macrophages Raw264.7 cells.
FIG. 3 is a graph showing NO (nitric oxide) secretion inhibitory activity of poesilochoricin-1 peptide.
4 is a graph showing the activity of inhibiting mRNA expression of IL-6 of the poesilochoricin-1 peptide.
5 is a graph showing the protein expression inhibitory activity of IL-6 of the poesilochoricin-1 peptide.
Figure 6 is a graph showing the inhibitory activity of mRNA expression of iNOS, COX-2 of the poesilochoricin-1 peptide.

Hereinafter, the present invention will be described in more detail through examples. These examples are only for illustrating the present invention, it will be apparent to those skilled in the art that the scope of the present invention is not limited by these examples.

<Example 1. Selection of peptide gene derived from clown stink bug>

Immunization of clown stink bugs was carried out by incubating Escherichia coli, Staphylococcus aureus, and Candida albicans in TSB (Tryptic Soy Broth, Difco, USA) liquid medium for 1 hour at 37°C and 200 rpm in a shaking incubator for 18 hours, then again under the same conditions. After incubation for 2 hours and 30 minutes, the cells are taken to be 5 × 10 ⁵ colony forming units (CFU) and injected into the body cavity using a micro-syringe and raised for 18 hours at 25°C to induce immunization. Did.

In order to maximize the expression of the bioactive substance, RNA-seq was performed using total RNA of normal and immunized clown stink bugs. First of all, to prepare the normal clown stink bug and immunized clown stink bug, to keep the tissue as fresh as possible, rapidly freeze it with liquid nitrogen, grind it into a mortar, prepare a sample, mix it with 100 mg of sample and 1 ml of TRIZOL and mix at room temperature for 5 minutes To react. After this, 200 µl chloroform was added and mixed, followed by reaction at room temperature for 3 minutes. Next, after centrifugation at 12,000×g for 15 minutes at 4°C, the supernatant was taken, 500 µl isopropanol was added and reacted at room temperature for 10 minutes, followed by centrifugation at 4°C for 12,000×g for 10 minutes. The precipitated total RNA was washed with 1 ml of 75% (v/v) ethanol aqueous solution and centrifuged at 4°C and 7,500×g for 5 minutes. After centrifugation, ethanol was removed and dried, and then dissolved in sterile water to prepare RNA. Prepared total RNA was confirmed by using the Agilent 2100 Bioanalyzer instrument RNA purity and quality.

Using the RNA thus obtained, genetic information on transcript transcripts was confirmed by RNA seq analysis using an Illumina HiSeq™ 2000 instrument. Existing bioactive peptide properties based on the sequence of amino acids translated from each transcript. The whole unigene was filtered with reference to the results, and as a result, a gene estimated as a new bioactive peptide was selected. The selected amino acid sequence was composed of 17 amino acids as KKRKKKAFALKFVVDLI-NH ₂ and was named Poecilocorisin-1 (Table 1).

Peptide Amino acid sequence Poecilocorisin-1 KKRKKKAFALKFVVDLI-NH ₂

<Example 2. Synthesis and separation and purification of poesilochoricin-1>

The poesilocolysin-1 peptide derived from the clown stink bug identified in Example 1 was synthesized and separated and purified.

First, in order to synthesize the poesilocolysine-1 peptide, the present inventors used the liquid phase solid-phase method of Merrifield (Merrifield, RB., J. Am. Chem. Soc., 85, using a Fmoc amino group protective container) 2149, 1963).

The peptide synthesis method was synthesized by a solid phase method using Fmoc (9-fluorenylmethoxycarbonyl) as a protecting group of an N _α -amino group of amino acids.

Specifically, a peptide having a carboxyl terminus -NH ₂ type was used as Rink Amide MBHA-Resin as a starting material, and a peptide having a carboxyl terminus -OH type was using Fmoc-amino acid-Wang Resin as a starting material.

The elongation of the peptide chain by coupling of Fmoc-amino acids was by DCC ( N -hydroxybenzo-triazole (HOBt)-dicyclo-hexylcar-bodiimide) method.

After coupling the Fmoc-amino acid at the amino terminal of each peptide, the Fmoc group is removed with 20% piperidine/N-methylpyrrolidone (NMP) solution, washed several times with NMP and dichloromethane (DCM), and then nitrogen Gas dried.

Trifluoroacetic acid (TFA)-phenol-thioanisole-H ₂ O-triisop-ropylsilane (85: 5: 5: 2.5: 2.5, vol./vol.) solution was added thereto and reacted for 3 hours to remove the protecting group from the resin. The peptide was isolated, and then the peptide was precipitated with diethyl ether. The crude peptide obtained in this way was purified with an acetonitrile gradient containing 0.1% TFA to form a purified reverse phase-HPLC column (Delta Pak, C ₁₈ 300Å, 15μm, 19.0 mm x 30mm, Waters).

After the synthetic peptide was hydrolyzed with 6 N-HCl at 110° C. for 24 hours, the obtained residue was concentrated under reduced pressure, and dissolved in 0.02 N-HCl to measure the amino acid composition with an amino acid analyzer (Hitachi 8500 A).

In addition, the molecular weight was calculated based on the sequence of the synthesized peptide, and the correct molecular weight was measured using a MALDI mass spectrometry (matrix-assisted laser desorption ionization mass spectrometer).

As a result, since the measured molecular weight and the calculated molecular weight matched, it was confirmed that an antibacterial peptide having an accurate amino acid sequence was synthesized.

<Example 3. Antibacterial and antifungal activity assay of poesilochoricin-1>

The antimicrobial activity assay for poesilochoricin-1 was confirmed using a RDA (radial diffusion assay) experimental method. The RDA method is a bacterium cultured in a sterile underlay gel composed of Citrate phosphate buffer (9 mM sodium phosphate, 1 mM sodium citrate, pH 7.4) and 1% (w/v) type I (low electroendosmosis) agarose, 0.03% TSB. Add (4 × 10 ⁶ colony forming units), mix and pour into a square plate. When the underlay gel is hardened, make a hole with a diameter of 3 mm and load the peptide into the hole at a concentration of 5 μl. After incubating at 37° C. for 3 hours so that the peptides spread evenly, 10 ml of overlay agar (6% TSB, 1% agarose) was poured and incubated again at 37° C. to confirm the clear zone and measure the diameter. The strains used were Gram-negative Escherichia coli , Gram-positive fungus Staphylococcus aureus , and Candida albicans as fungi.

The results for this are shown in FIG. 1, and the unit unit of FIG. 1 indicates a value represented by converting 1 mm in diameter of an antibacterial ring into 10 units.

Referring to FIG. 1, the peptide of the present invention, poesilochoricin-1, had a concentration-dependent antibacterial/antifungal effect on all tested bacteria or fungi, and in particular, it was found to be excellent in gram negative and gram positive bacteria.

<Example 4. Confirmation of cell viability of poesilochoricin-1>

MTS assay method using Raw264.7 cells, mouse macrophages Cytotoxicity was confirmed. For this, Raw264.7 cells were cultured and tested using DMEM medium containing antibiotics (100 units/mL penicillin, 100 μg/mL streptomycin) and 10% fetal bovine serum (FBS) in a 37°C, 5% CO ₂ incubator. Used for.

For MTS assay After dispensing 200 µl of 2×10 ⁴ cells/well cells in a 96-well culture container, the treatment was carried out for 24 hours in a concentration-dependent manner. After that, 10 μl of MTS reagent CellTiter 96 ^® AQueous One Solution Reagent (Promega, USA) was added and reacted for 3 to 4 hours to confirm the change in color, and the absorbance measurement at 450 nm was measured using a multi detecter (Beckman DTX8800, USA). It was confirmed through.

The results for this are shown in FIG. 2. Referring to FIG. 2, it was confirmed that poesilochoricin-1 was not toxic to Raw264.7 cells up to 100 µg/ml, and then at a concentration of 100 µg/ml or less. Experimented.

<Example 5. Assay of anti-inflammatory activity of poesilochoricin-1>

Example 5-1. NO (nitric oxide) secretion check

In order to measure the anti-inflammatory activity of poesilochoricin-1, the secretion of NO was confirmed in Raw264.7 cells. Raw264.7 cells are known to produce NO when secreting inflammation and secrete it out of the cell.

To confirm the secretion of NO, Raw264.7 cells were prepared in 6-well for each 1×10 ⁶ cells/ml cell number, and then the peptides were treated for 1 hour by concentration. After that, 1 μg of lipopolysaccharide (LPS) was treated to induce inflammation and cultured for 24 hours. 100 µl of the supernatant of the cultured cells was used for the experiment, and the amount of NO secreted by the LPS was reduced by the peptide using the NO detection kit (intron, Korea) using a multi detecter (Beckman DTX8800, USA). It was confirmed by absorbance measurement at 550nm wavelength.

The results for this are shown in FIG. 3, and referring to FIG. 3, it can be confirmed that the concentration of NO secretion decreases when treatment with a concentration of 25 μg/ml or more is carried out.

Example 5-2. Confirmation of IL-6 mRNA expression

When inflammation is induced in cells, the expression level of the cytokine, an inducer of inflammation, is increased. Accordingly, the expression level of IL-6, a representative substance among cytokines, was investigated using a qRT-PCR (Quantitative RT-PCR) method.

Raw264.7 cells were prepared in 6-wells with 1 × 10 ⁶ cells/ml cell count, respectively, and the peptides were treated for 1 hour by concentration. After that, 1 μg of LPS was treated to induce inflammation and cultured for 24 hours. Thereafter, the supernatant was removed, washed with PBS, and the cells were collected. 1 ml of TRIZOL solution was mixed with the collected cells and reacted at room temperature for 5 minutes. After mixing by adding 200 µL chloroform, centrifugation is performed at 4°C for 12,000×g for 15 minutes, supernatant is taken, 500 µl isopropanol is added, reacted for 10 minutes at room temperature, and then centrifuged at 4°C for 12,000×g for 10 minutes. Did. The precipitated RNA was washed with 1 ml 75% ethanol and centrifuged at 4°C and 7,500×g for 5 minutes. After centrifugation, ethanol was removed and dried, and then dissolved in sterile water to prepare RNA. Thereafter, cDNA was prepared with a cDNA synthesis kit using 1 μg of total RNA, and qRT-PCR experiments were performed. The primers used are shown in Table 2 below.

Name Sequence IL-6 Forward 5’-GAGGATACCACTCCCAACAGACC-3’ Reverse 5’-AAGTGCATCATCGTTGTTCATACA-3’ GAPDH Forward 5’-AAGGTCATCCCAGAGCTGAA-3’ Reverse 5’-CTGCTTCACCACCTTCTTGA-3’

The results of mRNA expression verification are shown in FIG. 4, and referring to FIG. 4, it can be seen that the mRNA expression level of IL-6 decreases due to the treatment of poesilochoricin-1. These results suggest that poesilochoricin-1 is a peptide capable of exhibiting an excellent effect on inflammatory diseases.

Example 5-3. Confirmation of protein expression of cytokine IL-6

Next, the protein expression level of IL-6 was examined using an ELISA (Enzyme-linked immunosorbent assay) test method.

Raw264.7 cells were prepared in 6-wells with 1 × 10 ⁶ cells/ml cell count, respectively, and the peptides were treated for 1 hour by concentration. After that, 1 μg of LPS was treated to induce inflammation and cultured for 24 hours. The supernatant of the cultured cells was collected, and the absorbance of IL-6 was measured and quantified using a multi-detector (Beckman DTX8800) using an ELISA kit.

The results for this are shown in FIG. 5. Referring to FIG. 5, it can be confirmed that the expression level of the IL-6 peptide was reduced due to the treatment with poesilochoricin-1.

Example 5-4. Confirmation of mRNA expression level of iNOS and COX-2

Next, using the primers in Table 3, the expression levels of the mRNAs of iNOS and COX-2, which are inflammatory mediators, were carried out in Example 5-2. Confirmed.

Name Sequence i-NOS Forward 5’-CAGCACAGGAAATGTTTCAGC-3’ Reverse 5’-TAGCCAGCGTACCGGATGA-3’ COX-2 Forward 5’-CAGACAACATAAACTGCGCCTT-3’ Reverse 5’-GATACACCTCTCCACCAATGACC-3’ GAPDH Forward 5’-AAGGTCATCCCAGAGCTGAA-3’ Reverse 5’-CTGCTTCACCACCTTCTTGA-3’

The results for this are shown in FIG. 6, and it can be seen that the mRNA expression of COX-2 and iNOS, which are the mediators of inflammation, is significantly reduced due to treatment with poesilochoricin-1.

<110> REPUBLIC OF KOREA(MANAGEMENT: RURAL DEVELOPMENT ADMINISTRATION) <120> Poecilocorisin-1 peptide isolated from Poecilocoris lewisi or antimicrobial, antimycotic and antiinflammatory composition comprising it <160> 1 <170> KoPatentIn 3.0 <210> 1 <211> 17 <212> PRT <213> Unknown <220> <223> Poecilocoris lewisi <400> 1 Lys Lys Arg Lys Lys Lys Ala Phe Ala Leu Lys Phe Val Val Asp Leu 1 5 10 15 Ile

Claims (11)

A peptide represented by the following SEQ ID NO: 1 synthesized from the gene of an antibacterial, antifungal or anti-inflammatory peptide isolated from a broad- leaved stink bug ( Poecilocoris lewisi ).
SEQ ID NO: KKRKKKAFALKFVVDLI-NH ₂ According to claim 1,
The peptide is a peptide characterized in that it exhibits antibacterial activity against any one or more of Staphylococcus aureus and Escherichia coli 0-157. According to claim 1,
The peptide is a peptide characterized in that it exhibits antifungal activity against Candida albicans . According to claim 1,
The peptide is a peptide characterized in that it inhibits the secretion of NO or IL-6, iNOS or COX-2 expression. An antimicrobial, antifungal or anti-inflammatory composition comprising the peptide of any one of claims 1 to 4 as an active ingredient. An antibiotic comprising the peptide of any one of claims 1 to 4 as an active ingredient. A food preservative comprising the peptide of any one of claims 1 to 4 as an active ingredient. Cosmetic preservative comprising the peptide of any one of claims 1 to 4 as an active ingredient. Pharmaceutical preservative comprising the peptide of any one of claims 1 to 4 as an active ingredient. A composition for the prevention or treatment of inflammatory diseases, comprising the peptide of any one of claims 1 to 4 as an active ingredient. The method of claim 10,
The inflammatory diseases include inflammatory bowel disease, inflammatory collagen vascular disease, glomerulonephritis, inflammatory skin disease, sarcoidosis, retinitis, gastritis, hepatitis, enteritis, arthritis, tonsillitis, sore throat, bronchitis, pneumonia, pancreatitis, sepsis, cystitis, nephritis and neuritis. A composition for the prevention or treatment of inflammatory diseases, which is selected from the group consisting of.

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