KR20220051080A - A protaetiamycine-4 peptide isolated from Protaetia brevitarsis seulensis larva and A use of the peptide - Google Patents

Abstract

The present invention relates to a peptide protaetiamycin-4 having an amino acid sequence of ACRRTMCVFCRRKWA-NH_2 derived from Protaetia brevitarsis seulensis and a use thereof. The protaetiamycin-4 has an excellent antibacterial or antifungal effect, thereby being used as a pharmaceutical composition for antibacterial or antifungal preparations, antibiotics, food preservatives, feed preservatives, cosmetic preservatives, or pharmaceutical preservatives.

Description

A protaetiamycine-4 peptide isolated from Protaetia brevitarsis seulensis larva and A use of the peptide

The present invention relates to a protetiamycin-4 peptide isolated from the larvae of white spot flower radish and its use, and more particularly, to a protetiamicin -4 peptide isolated from the larva of white spot flower radish ( Protaetia brevitarsis seulensis ) and to its antibacterial or antifungal use.

Infection of pathogenic microorganisms is one of the most common and fatal causes of human diseases. Unfortunately, antibiotic resistance of pathogenic microorganisms has been caused due to the abuse of antibiotics. Indeed, the rate at which pathogenic microorganisms develop resistance to new antibiotics is much faster than the rate at which analogues of new antibiotics are developed. For example, Enterococcus faecalis , Mycobacterium tuberculosis , Pseudomonas , which can be life-threatening aeruginosa ) and other pathogenic microorganisms have developed resistance to all known antibiotics.

Tolerance to antibiotics is a phenomenon distinct from resistance to antibiotics. It was first discovered in Pneumococcus sp. in the 1970s and provided important clues about the mechanism of action of penicillin. Resistant species stop growing in the presence of normal 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 synthetase. By activating it, it kills the bacteria, and the bacteria also suppress their activity, resulting in survival even in the case of antibiotic treatment.

It is very clinically important for pathogenic microorganisms to be resistant to antibiotics, because if it is impossible to eradicate the resistant microorganisms, the effectiveness of antibiotic treatment in clinical infections is reduced. In addition, the development of resistance is considered to be a prerequisite for the development of resistance to antibiotics, because it results in the surviving strains despite antibiotic treatment. These strains acquire new genetic elements that are resistant to antibiotics and continue to grow in the presence of antibiotics. Since pathogenic microorganisms showing practically all resistance are known to have resistance as well, the development of new antibiotics capable of killing pathogenic microorganisms having such antibiotic resistance is urgent.

As described above, it is necessary to develop a new antibiotic to prevent damage caused by pathogenic microorganisms that are resistant to antibiotics, and also to develop a new antibiotic that acts independently of autolysin activity. In addition, there is a need to provide a pharmaceutical composition for effectively treating infection of pathogenic microorganisms with such novel antibiotics.

On the other hand, some of the substances that play an important role in the process for maintaining homeostasis of an organism are physiologically active substances derived from various living organisms. Until now, many studies have been conducted on numerous physiologically active substances, and among them, antibacterial peptides isolated from various living organisms are known to act variously on bacteria, fungi, and viruses. Antimicrobial peptides are also known to play important roles in host defense and innate immune system. As related prior art, Korean Patent No. 10-0964136 (Antibacterial or antifungal peptide gene isolated from Uldo larvae and synthetic peptide with antibacterial or antifungal activity) and Korean Patent No. 10-1953828 (Antibacterial peptide derived from King cricket) Terogryleucine 1 and its composition) are known, but studies on peptides derived from White Spotted daisy and their novel uses are lacking until now.

The problem to be solved by the present invention is to prevent or treat diseases caused by bacteria such as gram-negative bacteria, gram-positive bacteria and fungi, and antibacterial isolated from white spot flower radish, which can be usefully used for applications requiring antibacterial, bactericidal and antifungal activity Or to provide a peptide protetiamicin-4 having antifungal properties and uses thereof.

The present invention is white-spotted flower radish ( Protaetia ) brevitarsis seulensis ) derived antibacterial or antifungal peptides and uses thereof.

In order to solve the above problems, the present invention provides a peptide represented by the following SEQ ID NO: 1 derived from larvae of Protaetia brevitarsis seulensis .

SEQ ID NO: 1: ACRRTMCVFCRRKWA-NH ₂

The method for providing the peptide according to the present invention is as follows. White-spotted flower radish ( Protaetia ) brevitarsis seulensis )-derived antibacterial or antifungal gene. First, the whole DNA is isolated by rapidly freezing the daikon radish in liquid nitrogen, and the whole genome sequencing method is used to determine the gene for the genus It includes a method of confirming information and selecting a candidate material through an antibacterial or antifungal activity test based on the sequence of amino acids translated from the genome.

In the present invention, "peptide", and "protein" are used interchangeably and include reference to a polymer of amino acid residues. The terms apply to natural amino acid polymers as well as amino acid polymers in which one or more amino acid residues are artificial chemical analogues of the corresponding natural amino acid. The terms also apply to those polymers containing conservative amino acid substitutions such that the protein remains functional. In the present invention, the peptide may be synthesized using a gene recombination and protein expression system, preferably synthesized in vitro through a peptide synthesizer or the like.

In the present invention, "biologically active" refers to a peptide fragment having a structural function similar to that of the polypeptide of SEQ ID NO: 1, and/or a similar regulatory function, and/or a similar biochemical function, and also a peptide according to the present invention. do.

The present invention may include a variant of the sequence of SEQ ID NO: 1. Specifically, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, Sequences having at least 98%, or at least 99% sequence homology and retaining biological activity may be included within the scope of the present invention.

In the present invention, a "deletion" is defined as a change in the nucleotide or amino acid sequence that lacks one or more nucleotide or amino acid residues, respectively, compared to a wild-type polynucleotide or polypeptide.

In the present invention, "insertion" or "addition" is a change in nucleotide or amino acid sequence resulting from the addition of one or more nucleotide or amino acid residues, respectively, compared to a wild-type polynucleotide or polypeptide.

In the present invention, "substitution" results from the replacement of one or more nucleotides or amino acids by different nucleotides or amino acids, respectively, compared to a wild-type polynucleotide or polypeptide.

On the other hand, preferred amino acid mutation at the substitution position may be performed based on the similarity of residues in polarity, charge, solubility, hydrophobicity, hydrophilicity and/or amphiphilic properties. For example, but not limited to, negatively charged amino acids include aspartic acid and glutamic acid; positively charged amino acids include lysine and arginine; And amino acids having an uncharged polar head group having a similar hydrophilicity value include leucine, isoleucine and valine; glycine and alanine; asparagine and glutamine; serine, threonine, phenylalanine and tyrosine; Such mutations may include conservative substitutions. A 'conservative substitution' refers to a substitution in which an amino acid is substituted with another amino acid having similar properties so that those skilled in the art can predict that the secondary structure and hydropathic nature (hydropathic nature) of the polypeptide are substantially unchanged. am. In general, the following groups of amino acids exhibit conservative changes: (1) ala, pro, gly, glu, asp, gln, asn, ser, thr; (2) cys, ser, tyr, thr; (3) val, ile, leu, met, ala, phe; (4) lys, arg, his; and (5) phe, tyr, trp, his.

In some cases, the variant is phosphorylation (phosphorylation), sulfation (sulfation), acrylation (acrylation), glycosylation (glycosylation), methylation (methylation), farnesylation (farnesylation), acetylation (acetylation) and amylation (amidation) It can also be modified (modification) and the like.

In addition, the sequence according to the present invention may further include a cell penetrating peptide sequence for intracellular penetration. The cell-penetrating peptide is a kind of signal peptide and is a peptide sequence for the purpose of delivering a substance into a cell. It mainly consists of a peptide sequence of about 7-30 amino acids, and any sequence having a signal peptide that can be delivered into a cell may be included in the present invention.

For example, the cell-penetrating peptide mainly contains basic amino acid residues such as lysine/arginine, and thus serves to penetrate the fused proteins into the cell membrane and into the cell. The cell-penetrating peptide is HIV-1 Tat protein, Drosophila antennapedia homeodomain (phenetratin), HSV VP22 transcriptional regulatory protein, vFGF-derived MTS peptide, PTD-5, transpotan or Pep-1 peptide Sequences derived from, but are not limited thereto. As such, various CPPs identified/synthesized from viruses or cationic peptides (eg, TAT48-60, penetratin (pAntp) 43-58, polyarginine, Pep-1, transpotan, etc.) are biologically active substances. has an activity capable of internalization of cells to mediate the movement of drug carriers.

The amino acid sequence of the peptide consists of 11 amino acids as ACRRTMCVFCRRKWA-NH ₂ , which is called protaetiamycine-4.

According to the present invention, since the peptide can exhibit excellent antibacterial or antifungal activity against Gram-positive bacteria, Gram-negative bacteria or fungi, it is useful as a pharmaceutical composition for an antibacterial or antifungal agent. The gram-positive or gram-negative bacteria are, for example, Escherichia coli , Pseudomonas aeruginosa , Staphylococcus aureus , Klebsiella pneumoniae , MRSA bacteria ( Staphylococcus aureus subsp. aureus ), Bacillus subtilis ). Bacillus subtilis ), Vibrio enteritis ( Vibrio parahaemolyticus ), Propionibacterium acnes ), Salmonella typhimurium ) or Shigella flexneri ) It may be, but is not limited thereto.

The fungus may be, for example, Candida albicans , but is not limited thereto.

According to the present invention, the peptide is characterized in that it is non-toxic to cells. The cells may be, for example, mouse red blood cells, but are not limited thereto. In one embodiment of the present invention, it was confirmed that the peptide according to the present invention did not show cytotoxicity as a result of treatment with mouse erythrocytes. Therefore, the peptide of the present invention can be usefully used as a safe antibacterial or antifungal agent.

The present invention provides an antibacterial or antifungal composition comprising a peptide having the amino acid sequence of SEQ ID NO: 1, protetiamycin-4 (Protaetiamycine-4).

SEQ ID NO: 1: ACRRTMCVFCRRKWA-NH ₂

In the present invention, the "antibacterial composition" or "antifungal composition" may have the same meaning as an antibiotic, which is a generic term for antimicrobial agents, and may have the same meaning as an antibacterial agent, an antifungal agent, a bactericide, an antiseptic, a preservative, or a bactericide. For example, bacteria that cause food poisoning or purulent infections, bacteria that can aggravate diseases due to infection when the resistance of the living body is low, such as surgery or burns, and bacteria that cause oral diseases or vaginitis It means a substance capable of blocking, inhibiting, or killing the growth and life function of pathogenic microorganisms.

In addition, the present invention provides an antibiotic comprising the peptide having the amino acid sequence of SEQ ID NO: 1, Protaetiamycine-4, as an active ingredient. Since the peptide protethiamicin-4 according to the present invention has antibacterial or antifungal activity against pathogenic microorganisms, particularly, pathogenic microorganisms having antibiotic resistance, it can be usefully used as an antibiotic.

The use of the antibiotic includes use as a pharmaceutical composition for the purpose of treatment or prophylaxis.

As used herein, "treatment" and "treating" refer to the administration or application of a therapeutic agent to a subject or the performance of a procedure or modality in a subject for the purpose of obtaining the benefit of treatment of a disease or health-related condition. “Prevention,” “preventing,” and the like refer to an approach for preventing, inhibiting, or reducing the likelihood of occurrence or recurrence of a disease or condition. It also refers to delaying the onset or recurrence of a disease or condition or delaying the onset or recurrence of a disease or condition.

In the present invention, “subject” and “patient” refer to a human or non-human, such as a primate, mammal, or vertebrate. In certain embodiments, the subject is a human.

In the present invention, "therapeutic benefit" or "therapeutically effective" refers to anything that promotes or enhances the health of a subject in connection with the medical treatment of such condition. This includes, but is not limited to, a decrease in the frequency or severity of signs or symptoms of a disease.

The protethiamicin-4 according to the present invention may be added to the pharmaceutical composition of the present invention in an amount of 0.001 to 95% by weight. The pharmaceutical composition may be formulated in the form of powders, granules, tablets, capsules, suspensions, emulsions, syrups, aerosols, etc., external preparations, suppositories, and sterile injection solutions according to conventional methods, respectively. Carriers, excipients and diluents that may be included in the pharmaceutical composition include lactose, dextrose, sucrose, sorbitol, mannitol, xylitol, erythritol, maltitol, starch, acacia gum, alginate, gelatin, calcium phosphate, calcium silicate, cellulose , methylcellulose, microcrystalline cellulose, polyvinyl pyrrolidone, water, methylhydroxybenzoate, propylhydroxybenzoate, talc, magnesium stearate and mineral oil. In the case of formulation, it is prepared using commonly used diluents or excipients such as fillers, extenders, binders, wetting agents, disintegrants, and surfactants. Solid preparations for oral administration include tablets, pills, powders, granules, capsules, etc., and such solid preparations include at least one excipient, for example, starch, calcium carbonate to the peptide protethiamicin-4 of the present invention. , sucrose or lactose, gelatin, etc. are mixed and prepared. In addition to simple excipients, lubricants such as magnesium stearate and talc are also used. Liquid formulations for oral use include suspensions, solutions, emulsions, syrups, etc. In addition to water and liquid paraffin, which are commonly used simple diluents, various excipients, for example, wetting agents, sweeteners, fragrances, preservatives, etc. may be included. . Formulations for parenteral administration include sterile aqueous solutions, non-aqueous solutions, suspensions, emulsions, freeze-dried preparations, and suppositories. Non-aqueous solvents and suspending agents include propylene glycol, polyethylene glycol, vegetable oils such as olive oil, and injectable esters such as ethyl oleate. As the base of the suppository, witepsol, macrogol, tween 61, cacao butter, laurin, glycerogelatin, and the like can be used.

The dosage of the pharmaceutical composition of the present invention will vary depending on the age, sex, and weight of the subject to be treated, the specific disease or pathological condition to be treated, the severity of the disease or pathological condition, the route of administration, and the judgment of the prescriber. Dosage determination based on these factors is within the level of one of ordinary skill in the art, and generally dosages range from 0.01 mg/kg/day to approximately 2000 mg/kg/day. A more preferred dosage is 1 mg/kg/day to 500 mg/kg/day. Administration may be administered once a day, or may be administered in several divided doses. The above dosage does not limit the scope of the present invention in any way.

The pharmaceutical composition of the present invention may be administered to mammals such as mice, livestock, and humans by various routes. Any mode of administration can be envisaged, for example, by oral, rectal or intravenous, intramuscular, subcutaneous, intrauterine dural or intracerebrovascular injection. The pharmaceutical composition of the present invention is suitable for parenteral administration, including intravenous or body cavity administration.

In addition, the present invention provides an antibacterial or antifungal external preparation for skin containing protetiamycin-4 (Protaetiamycine-4), which is a peptide having the amino acid sequence of SEQ ID NO: 1. Since the peptide protethiamicin-4 according to the present invention has antibacterial activity against gram-positive or gram-negative bacteria and has antifungal activity against fungi, it can be usefully used as an antibacterial or antifungal external preparation for skin.

In addition, the present invention provides a food preservative, feed preservative, cosmetic preservative, and pharmaceutical preservative comprising the peptide protethiamicin-4. At this time, food preservatives, feed preservatives, cosmetic preservatives, and pharmaceutical preservatives are additives used to prevent deterioration, spoilage, discoloration and chemical changes of food, feed, pharmaceuticals, and cosmetics. Functional antibiotics such as inhibiting the growth of microorganisms such as yeast and inhibiting the growth or sterilization of putrefactive microorganisms in food or pharmaceuticals are also included. Ideal conditions for these food preservatives, cosmetics or pharmaceutical preservatives should be non-toxic and effective even in trace amounts.

In particular, since the novel peptide protethiamicin-4 of the present invention exhibits antibacterial or antifungal activity and has minimal toxicity, it can be usefully used as a preservative for food or feed, as a preservative for cosmetics or pharmaceuticals.

The use of the above food or feed as a preservative is to be additionally added to materials for general food or feed, and there is no limitation on the type of food or feed.

For use as a preservative in cosmetics or pharmaceuticals as described above, substances selected arbitrarily according to the purpose of use, etc. may be added. For example, purified water, oil, surfactant, humectant, higher alcohol, thickener, chelating agent, pigment, fatty acid, wax, pH adjuster, fragrance, etc. may be added.

In addition, the peptide according to the present invention can be used for various purposes and uses requiring antibacterial, bactericidal or antifungal activity. Specifically, it can be used as a skin cleaner, hair cleaner, vaginal cleaner, mouthwash, bathroom cleaner, kitchen cleaner, food additive, feed additive, disinfectant or humidifier disinfectant material.

As a food and/or feed preservative, cosmetic or pharmaceutical preservative, skin cleaner, hair cleaner, vaginal cleaner, mouthwash, bathroom cleaner, kitchen cleaner, food additive, feed additive, disinfectant or humidifier disinfectant material, etc. In this case, the peptide may be included in an amount of 0.00001 to 50% by weight based on the total weight of the additive, and may be included in a concentration of 1 μg/ml to 10000 μg/ml. In addition, other known antibacterial substances having additional antibacterial activity or substances capable of imparting other functionality may be further included.

Peptide protetiamicin-4 derived from white spot flower radish according to the present invention has almost no cytotoxicity and exhibits excellent antibacterial or antifungal activity. It can be usefully applied as a preservative or the like.

1 shows the results of antibacterial and antifungal activity of protetiamicin-4 according to the present invention.
Figure 2 shows the cytotoxicity test results of protetiamicin-4 according to the present invention.

Hereinafter, preferred examples are presented to help the understanding of the present invention, but the following examples are merely illustrative of the present invention, and it will be apparent to those skilled in the art that various changes and modifications are possible within the scope and spirit of the present invention, It goes without saying that such variations and modifications fall within the scope of the appended claims.

< Example 1. Preparation of peptide protetiamicin-4 having the amino acid sequence of SEQ ID NO: 1 (Protaetiamycine-4)>

experimental insect

White-spotted flower radish ( Protaetia ) brevitarsis seulensis ) was bred in the insect breeding building of the National Academy of Agricultural Sciences, using fermented sawdust as a food source, and was bred in a photoperiod of 16L:8D under conditions of 28℃ and 70% relative humidity.

Genomic DNA Isolation

Sequencing was carried out using the genome (genomic) of the white-spotted larvae. First, after preparing the white-spotted larvae, the intestines are dissected and frozen in liquid nitrogen to keep the tissues except the intestines as fresh as possible, and the samples are prepared by grinding them in a mortar, then 20 mg of the sample and Nuclei It was mixed with 600 μl of Lysis Solution and reacted on ice. After homogenization using a pestle, it was reacted at 65° C. for 30 minutes. Next, 3 μl of RNase solution was added for RNA removal, and after reacting at 37°C for 30 minutes, 200 μl of Protein Precipitation Solution was added and mixed, followed by reaction on ice for 5 minutes. Next, centrifuged at 16,000 × g for 4 minutes, and the supernatant was mixed with 600 μl of isopropyl alcohol (isopropanol) and reacted. Next, centrifuged at 16,000 × g for 1 minute, and the precipitated DNA was washed with 600 μl of 70% ethanol and centrifuged at 16,000 × g for 1 minute. After centrifugation, ethanol was removed, dried, and dissolved in sterile water to prepare DNA. The prepared DNA was subjected to absorbance and electrophoresis to confirm the purity and quality of the DNA.

gene selection

DNA analysis was performed on the larvae sample prepared for genome sequencing using a PacBio device, and as a result, genes presumed to be anti-inflammatory peptides were selected. The selected amino acid sequence is ACRRTMCVFCRRKWA-NH ₂ , and consists of 15 amino acid sequences, and was named as Protaetiamycine-4.

< test example 1. Evaluation of antibacterial/antifungal activity against pathogenic microorganisms>

RDA (radial diffusion assay) was performed to evaluate the antibacterial activity of the peptide protetiamicin-4 against pathogenic microorganisms. In the present invention, the antibacterial peptide was stored at -20 ℃, dissolved in sterile tertiary distilled water and used.

<Antibacterial activity assay>

For the antimicrobial activity assay, first the pathogenic bacteria Staphylococcus aureus and Escherichia coli ) in 3% (w/v) TSB (trypticase soy broth) at 37° C., 200 rpm for 18 hours, then incubated again for 2 hours and 30 minutes to become log-phase under the same conditions. .

Next, 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 cultured bacteria (4×10 ⁶ colony forming units/ml) to (underlay gel) and mix, pour on a square plate, and when the underlay gel hardens, make a hole 3 mm in diameter by concentration (0, 12.5, 25, 50, 100 and 200 μg/ml) of the peptide (protetiamicin-4) was introduced into the wells in 5 μl increments.

After incubation at 37°C for 3 hours to spread the peptide, 10 ml of overlay gel (6% TSB, 1% agarose) was poured, and the diameter of the clear zone was measured by incubation at 37°C again. 1 is shown

As shown in Figure 1, the peptide protethiamicin-4 was found to have activity against E. coli and Staphylococcus aureus, and the antibacterial activity was shown to increase in a concentration-dependent manner. Through this, it was confirmed that the peptide protetiamicin-4 according to the present invention has high availability as a therapeutic agent for known harmful strains and has excellent antibacterial activity.

< Antifungal Activity Assay >

For the measurement of the antifungal activity of the peptide, the pathogenic fungus Candida albicans was grown overnight at 30° C., 200 rpm in TSB medium (trypticase soy broth), and then inoculated in a new medium and grown for 3 hours. it was made to be gigantic.

Next, a sterile underlay consisting of citrate phosphate buffer (9 mM sodium phosphate, 1 mM sodium citrate, pH7.4) and 1% (w/v) type I (low electroendosmosis) agarose, 0.03% TSB. After adding the cultured bacteria (4×10 ⁶ colony forming units/ml) to the gel and mixing it, pour it on a square plate. When the underlay gel hardens, a hole with a diameter of 3 mm is made by concentration (0, 12.5). , 25, 50, 100, and 200 μg/ml) of the peptide (protetiamicin-4) was placed in 5 μl of each hole.

After incubation at 37°C for 3 hours to spread the peptide, 10 ml of overlay gel (6% TSB, 1% agarose) was poured, and the diameter of the clear zone was measured by incubation at 37°C again. 1 is shown.

As shown in FIG. 1 , the peptide protetiamicin-4 also exhibited antifungal activity against Candida albicans, and it was found that the antifungal activity increased in a concentration-dependent manner with protetiamycin-4. Through this, it was confirmed that the peptide protetiamicin-4 according to the present invention has excellent antifungal activity.

Through this, it was confirmed that the peptide protethiamicin-4 according to the present invention exhibits a wide range and excellent antibacterial and antifungal activity.

< test example 2. Cytotoxicity test>

A hemolysis assay was performed to investigate the cytotoxicity of the protetiamicin-4 peptide. For cells, mouse erythrocytes were washed three times with phosphate-sodium chloride buffer, pH=7.4 (PBS), and then diluted with phosphate-sodium chloride buffer to prepare a 5.00% erythrocyte solution. Next, 100 μl of 5.0% red blood cell solution was dispensed into each tube, and protetiamicin-4 was treated at different concentrations (0, 12.5, 25, 50, 100 and 200 μg/ml) for 24 hours. Phosphate-sodium chloride buffer, pH=7.4 (PBS) was added to all tubes so that the total amount was 200 μl, and incubated for 30 minutes in a 37°C incubator. After incubation, centrifugation was performed for 10 minutes at a rotation speed of 1000 rpm in a centrifuge, and the supernatant was transferred to a 96-well culture vessel, and absorbance was measured at a wavelength of 550 nm using a multi detector (Beckman DTX8800). As a control, the value when treated with 1% Triton X-100 was calculated as 100% destructive capacity, and when only red blood cells were added, 0% destructive capacity was calculated. At this time, the destructive ability of the peptide was calculated by the following equation.

[Equation 1]

% destruction ability = (absorbance of peptide-treated solution 550 nm - absorbance of phosphate-sodium chloride buffer 550 nm) / (absorbance of solution treated with Triton X-100 550 nm - absorbance of phosphate-sodium chloride buffer 550 nm) × 100

As shown in FIG. 2 , the peptide protethiamicin-4 showed insignificant ability to destroy red blood cells even when treated at a high concentration up to 200 μg/ml. On the other hand, melittin, a strong antibacterial peptide used as a control, was evaluated to have high cytotoxicity even at low concentrations.

Through this, the peptide protetiamicin-4 according to the present invention has minimal cytotoxicity, so it can be used as a safe antibacterial, antifungal and antibiotic, as well as useful as a food or feed preservative, and cosmetic or pharmaceutical preservative. did

<110> REPUBLIC OF KOREA (MANAGEMENT : RURAL DEVELOPMENT ADMINISTRATION) <120> A protaetiamycine 4 peptide isolated from Portaetia brevitarsis seulensis larva and A use of the peptide <130> NSH1-154 <160> 1 <170> KoPatentIn 3.0 <210> 1 <211> 15 <212> PRT <213> Artificial Sequence <220> <223> Protaetia brevitarsis seulensis <400> 1 Ala Cys Arg Arg Thr Met Cys Val Phe Cys Arg Arg Lys Trp Ala 1 5 10 15

Claims (12)

A peptide represented by SEQ ID NO: 1 below:
SEQ ID NO: 1: ACRRTMCVFCRRKWA-NH ₂ According to claim 1,
Wherein the peptide exhibits antibacterial or antifungal activity. According to claim 1,
The peptides are Escherichia coli , Pseudomonas aeruginosa , Staphylococcus aureus , Klebsiella pneumoniae , MRSA Staphylococcus aureus subsp . aureus ), Bacillus subtilis ( Bacillus subtilis ), enteritis vibrio ( Vibrio ) parahaemolyticus ), Propionibacterium acnes ( Propionibacterium acnes ), Salmonella typhimurium ), Shigella flexneri ) and Candida albicans ) The peptide that exhibits antibacterial or antifungal activity against any one or more selected from the group consisting of. Antibacterial or antifungal composition comprising the peptide protetiamycin-4 (Protaetiamycine-4) having the amino acid sequence of SEQ ID NO: 1. 5. The method of claim 4,
Escherichia coli , Pseudomonas aeruginosa , Staphylococcus aureus , Klebsiella pneumoniae , MRSA Staphylococcus aureus subsp. aureus , Bacillus subtilis , Bacillus subtilis Vibrio parahaemolyticus ), Propionibacterium acnes ), Salmonella typhimurium ) and Shigella flexneri ) The composition that exhibits antibacterial activity against any one or more selected from the group consisting of. 5. The method of claim 4,
A composition that exhibits antifungal activity against Candida albicans . An antibiotic comprising the peptide protetiamycin-4 (Protaetiamycine-4) having the amino acid sequence of SEQ ID NO: 1 as an active ingredient. An antibacterial or antifungal external preparation for skin comprising the peptide of any one of claims 1 to 3. A food preservative comprising the peptide of any one of claims 1 to 3. A feed preservative comprising the peptide of any one of claims 1 to 3. A cosmetic preservative comprising the peptide of any one of claims 1 to 3. A pharmaceutical preservative comprising the peptide of any one of claims 1 to 3.

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