KR102496847B1 - A protaetiamycine-5 peptide isolated from Protaetia brevitarsis seulensis larva and A use of the peptide - Google Patents

Abstract

The present invention relates to a peptide proteiamycin-5 having an amino acid sequence of WVIILAKQTKIVKIK-NH ₂ derived from white-spotted rhododendron and its use. Since proteiamycin-5 has excellent antibacterial or antifungal effect, It can be used as a pharmaceutical composition for preparation, antibiotic, food preservative, feed preservative, cosmetic preservative or pharmaceutical preservative.

Description

A protaetiamycin-5 peptide isolated from Protaetia brevitarsis seulensis larva and A use of the peptide}

The present invention relates to a proteiamycin-5 peptide isolated from larvae of white-spotted flower radish and its use, and more particularly, to a protetiamicin -5 peptide isolated from larvae of white-spotted flower radish ( Protaetia brevitarsis seulensis ) and It relates to its antibacterial or antifungal use.

Infection with pathogenic microorganisms is one of the most common and fatal causes of human disease. Unfortunately, due to the overuse of antibiotics, resistance of pathogenic microorganisms to antibiotics has been caused. In fact, 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 , which can pose a threat to life, Mycobacterium tuberculosis , Pseudomonas aruginosa ( Pseudomonas ) aeruginosa ) have developed resistance to all known antibiotics.

Tolerance to 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 normal concentrations of antibiotics, but do not die as a result. This resistance occurs because when antibiotics inhibit cell wall synthase, the activity of bacterial autolytic enzymes such as autolysin does not occur. By activating, it kills bacteria, and bacteria also suppress their activity, resulting in survival even when treated with antibiotics.

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

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

On the other hand, some of the substances that play an important role in the process for maintaining the homeostasis of living organisms 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 in a variety of ways, ranging from bacteria, fungi and viruses. Antimicrobial peptides are also known to play an important role in host defense and the innate immune system. As related prior art, Korean Patent No. 10-0964136 (antibacterial or antifungal peptide gene isolated from Uldo larvae and synthetic peptide having antibacterial or antifungal activity) and Korean Patent No. 10-1953828 (antibacterial peptide derived from king cricket) terogryleucine 1 and compositions thereof) are known, but studies on peptides derived from white-spotted daisies and new uses thereof are lacking.

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 to use antibacterial, bactericidal, and antifungal activities. Or to provide a peptide proteiamycin-5 having antifungal properties and its use.

The present invention is a white-spotted flower ( Protaetia brevitarsis seulensis ) and its use.

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

SEQ ID NO: 1: WVIILAKQTKIVKIK-NH ₂

A method for providing the peptide according to the present invention is as follows. white-spotted flower ( Protaetia brevitarsis seulensis ) in order to identify the derived antibacterial or antifungal gene, first, rapidly freeze the white-spotted radishes in liquid nitrogen to isolate the entire DNA, and use the whole genome sequencing method to identify the genes related to the genome of the white-spotted radishes. It includes a method of checking information and selecting candidates through antibacterial or antifungal activity tests based on amino acid sequences translated from the genome.

In the present invention, "peptide" and "protein" are used interchangeably and include reference to polymers 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 acids. The terms also apply to those polymers that contain conservative amino acid substitutions such that the protein remains functional. In the present invention, the peptide may be synthesized using genetic recombination and a protein expression system, preferably synthesized in vitro through a peptide synthesizer or the like.

In the present invention, "biologically active" means 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, as well as 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% with the peptide sequence of SEQ ID NO: 1, Sequences that have at least 98%, or at least 99% sequence homology, that retain biological activity may be included within the scope of the present invention.

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

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

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

On the other hand, a preferred amino acid change at a substitution site may be one performed based on the similarity of polarity, charge, solubility, hydrophobicity, hydrophilicity and/or amphiphilic properties of the residues. 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 uncharged polar head groups having similar hydrophilicity values 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' is a substitution in which an amino acid is substituted with another amino acid having similar properties, and those skilled in the art can predict that the secondary structure and hydropathic nature (hydropathic nature, hydrophobic or hydrophilic 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, sulfation, acrylation, glycosylation, methylation, farnesylation, acetylation and amylation It can also be modified as

In addition, the sequence according to the present invention may further include a cell penetrating peptide sequence for intracellular penetration. A cell-penetrating peptide is a kind of signal peptide, which is a peptide sequence intended to transmit substances into cells. It mainly consists of 7-30 amino acid peptide sequences, and any sequence may be included in the present invention as long as it has a signal peptide that can be delivered into cells.

For example, cell-penetrating peptides mainly contain basic amino acid residues such as lysine/arginine, and thus allow proteins fused thereto to permeate cell membranes and enter cells. The cell-penetrating peptide is HIV-1 Tat protein, Drosophila antennapedia homeodomain (Penetratin), HSV VP22 transcriptional regulatory protein, vFGF-derived MTS peptide, PTD-5, transportan or Pep-1 peptide Including sequences derived from, and the like, but are not limited thereto. As such, various CPPs (e.g., TAT48-60, penetratin (pAntp) 43-58, polyarginine, Pep-1, transportan, etc.) identified/synthesized from viruses or cationic peptides are biologically active substances. has an activity capable of internalizing cells to mediate the movement of drug carriers.

The amino acid sequence of the peptide is WVIILAKQTKIVKIK-NH ₂ and is composed of 11 amino acids, which is named Protaetiamycin-5.

According to the present invention, the peptide can exhibit excellent antibacterial or antifungal activity against gram-positive bacteria, gram-negative bacteria or fungi, so it is useful as a pharmaceutical composition for antibacterial or antifungal preparations. The gram-positive or gram-negative bacteria are, for example, Escherichia coli , Pseudomonas aeruginosa , Staphylococcus aureus , Klebsiella pneumoniae , MRSA ( Staphylococcus aureus subsp. aureus ), Bacillus subtilis ( Bacillus subtilis ), Vibrio parahaemolyticus , Propionibacterium acnes , Salmonella typhimurium , or Shigella flexneri , 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 exhibit cytotoxicity as a result of treating 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 Protaetiamycin-5, which is a peptide having the amino acid sequence of SEQ ID NO: 1 below.

SEQ ID NO: 1: WVIILAKQTKIVKIK-NH ₂

In the present invention, the "antibacterial composition" or "antifungal composition" may mean the same as antibiotics, which is a generic term for antimicrobial agents, and may mean the same as antibacterial agents, antifungal agents, bactericides, preservatives, preservatives, or disinfectants. For example, bacteria that cause food poisoning or cause purulent infections, bacteria that can aggravate diseases due to infection when the body's resistance is lowered, such as surgery and burns, and bacteria that cause oral disease or vaginitis It means a substance capable of inhibiting, suppressing 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, Protaetiamycin-5 (Protaetiamycine-5) as an active ingredient. Since the peptide protethiamycin-5 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.

Use as the antibiotic includes use as a pharmaceutical composition for the purpose of treatment or prevention.

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 a therapeutic benefit for 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 development or recurrence of a disease or condition.

In the present invention, “subject” and “patient” refer to humans or non-humans, such as primates, mammals, and vertebrates. 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 with respect to medical treatment of such a condition. This includes, but is not limited to, a reduction in the frequency or severity of signs or symptoms of a disease.

The protethiamycin-5 according to the present invention may be added in an amount of 0.001 to 95% by weight in the pharmaceutical composition of the present invention. The pharmaceutical composition may be formulated and used in the form of oral formulations such as powders, granules, tablets, capsules, suspensions, emulsions, syrups, aerosols, 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, gum acacia, alginate, gelatin, calcium phosphate, calcium silicate, and cellulose. , methylcellulose, microcrystalline cellulose, polyvinyl pyrrolidone, water, methylhydroxybenzoate, propylhydroxybenzoate, talc, magnesium stearate and mineral oil. When formulated, it is prepared using diluents or excipients such as commonly used fillers, extenders, binders, wetting agents, disintegrants, and surfactants. Solid preparations for oral administration include tablets, pills, powders, granules, capsules, etc. These solid preparations contain at least one excipient, for example, starch, calcium carbonate, in addition to the peptide proteiamycin-5 of the present invention. It is prepared by mixing sucrose or lactose, gelatin, etc. In addition to simple excipients, lubricants such as magnesium stearate and talc are also used. Liquid preparations for oral use include suspensions, solutions for oral use, emulsions, syrups, etc. In addition to water and liquid paraffin, which are commonly used simple diluents, various excipients such as wetting agents, sweeteners, aromatics, and preservatives may be included. . Formulations for parenteral administration include sterilized aqueous solutions, non-aqueous solvents, suspensions, emulsions, freeze-dried formulations, and suppositories. Propylene glycol, polyethylene glycol, vegetable oils such as olive oil, and injectable esters such as ethyl oleate may be used as non-aqueous solvents and suspensions. As a base for the suppository, witepsol, macrogol, tween 61, cacao butter, laurin paper, glycerogeratin and the like may 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. Determination of dosage based on these factors is within the level of those skilled 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 dosage is not intended to limit the scope of the present invention in any way.

The pharmaceutical composition of the present invention can be administered to mammals such as rats, livestock, and humans through various routes. All modes of administration are contemplated, eg oral, rectal or intravenous, intramuscular, subcutaneous, intrauterine intrathecal or intracerebrovascular injection. The pharmaceutical composition of the present invention is suitable for parenteral administration, including intravenous administration or intracorporeal administration.

In addition, the present invention provides an antibacterial or antifungal skin external preparation comprising Protaetiamycin-5, which is a peptide having the amino acid sequence of SEQ ID NO: 1. Since the peptide protethiamycin-5 according to the present invention has antibacterial activity against gram-positive or gram-negative bacteria and antifungal activity against fungi, it can be usefully used as an external skin preparation for antibacterial or antifungal use.

In addition, the present invention provides a food preservative, a feed preservative, a cosmetic preservative, and a pharmaceutical preservative containing the peptide proteiamycin-5. At this time, food preservatives, feed preservatives, cosmetic preservatives, and pharmaceutical preservatives are additives used to prevent deterioration, decay, discoloration, and chemical changes in food, feed, medicines, and cosmetics, and include disinfectants and antioxidants, and include bacteria, fungi, Also included are functional antibiotics, such as suppressing the growth of microorganisms such as yeast, inhibiting the growth of spoilage microorganisms in food or medicine, or sterilizing action. Ideal conditions for such food preservatives, cosmetics or pharmaceutical preservatives should be non-toxic and effective even in small amounts.

In particular, since the novel peptide proteiamycin-5 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, or as a preservative for cosmetics or pharmaceuticals.

The use of the above food or feed as a preservative is added to general food or feed materials, and there is no limit to the type of food or feed.

For use as a cosmetic or pharmaceutical preservative as above, a substance selected arbitrarily may be added according to the purpose of use. For example, purified water, oil, a surfactant, a moisturizer, a higher alcohol, a thickener, a chelating agent, a pigment, a fatty acid, a wax, a pH adjuster, and a flavoring agent 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 sterilizer material.

For use as above-mentioned food and/or feed preservatives, cosmetics or pharmaceutical preservatives, skin cleaners, hair cleaners, vaginal cleaners, mouthwashes, bathroom cleaners, kitchen cleaners, food additives, feed additives, disinfectants, or materials for humidifier disinfectants, etc. In the 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 functionalities may be further included.

Since the peptide proteiamycin-5 derived from white-spotted daisies according to the present invention has almost no cytotoxicity and exhibits excellent antibacterial or antifungal activity, it can be used as an antibacterial or antifungal pharmaceutical composition, antibiotic, food or feed preservative, cosmetic or pharmaceutical product. It can be usefully applied as a preservative and the like.

Figure 1 shows the antibacterial and antifungal activity results of protethiamycin-5 according to the present invention.
Figure 2 shows the results of the cytotoxicity test of proteiamycin-5 according to the present invention.

Hereinafter, preferred embodiments are presented to aid understanding of the present invention, but the following examples are merely illustrative of the present invention, and various changes and modifications are possible within the scope and spirit of the present invention. It is obvious to those skilled in the art, It goes without saying that these variations and modifications fall within the scope of the appended claims.

< Example 1. Preparation of peptide proteiamycin-5 having the amino acid sequence of SEQ ID NO: 1 >

experimental insect

White-spotted flower ivy ( Protaetia brevitarsis seulensis ) used fermented sawdust as a food source in the insect breeding wing of the National Institute of Agricultural Sciences, and was bred at 28℃ and 70% relative humidity at a photoperiod of 16L:8D.

Genomic DNA isolation

Sequencing was performed using the genome of the white-spotted radish larvae. First, after preparing the white-spotted larvae, the intestines were removed by dissection, rapidly frozen in liquid nitrogen to keep the tissues excluding the intestines as fresh as possible, and prepared by grinding in a mortar and pestle, 20 mg of sample and Nuclei It was mixed with 600 μl of Lysis Solution and reacted on ice. After homogenization using a pestle, the mixture was reacted at 65° C. for 30 minutes. Next, 3 μl of RNase solution was added to remove RNA, reacted at 37 ° C for 30 minutes, 200 μl of Protein Precipitation Solution was added, mixed, and reacted on ice for 5 minutes. Next, centrifugation was performed at 16,000 × g for 4 minutes, and the supernatant was taken and reacted by mixing with 600 μl of isopropanol. Next, centrifugation was performed 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 confirmed for its purity and quality through absorbance and electrophoresis.

gene selection

DNA analysis was performed on the larvae of the white-spotted flower radish 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 was WVIILAKQTKIVKIK-NH ₂ and was composed of 15 amino acid sequences, and was named Protaetiamycin-5.

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

Radial diffusion assay (RDA) was performed to evaluate the antibacterial activity of the peptide proteiamycin-5 against pathogenic microorganisms. In the present invention, the antimicrobial peptide was stored at -20 ° C and used after being dissolved in sterilized tertiary distilled water.

<Antibacterial activity assay>

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

Next, a sterilized underlay gel consisting of citrate phosphate buffer (9 mM sodium phosphate, 1 mM sodium citrate, pH 7.4), 1% (w/v) type I (low electroendosmosis) agarose, and 0.03% TSB Cultured bacteria (4×10 ⁶ colony forming units/ml) are added to (underlay gel), mixed, poured into a square plate, and when the underlay gel is hardened, a hole with a diameter of 3 mm is made and divided according to concentration (0, 12.5, 25, 50, 100, and 200 μg/ml) of the peptide (Proteiamycin-5) was put into the hole at 5 μl each.

After incubation at 37 ° C. for 3 hours to diffuse the peptide, 10 ml of overlay gel (6% TSB, 1% agarose) was poured and incubated again at 37 ° C. to measure the diameter of the clear zone. shown in Figure 1

As shown in FIG. 1, the peptide proteiamycin-5 was found to be active against Escherichia coli and Staphylococcus aureus, and the antibacterial activity was found to increase in a concentration-dependent manner. Through this, it was confirmed that the peptide proteiamycin-5 according to the present invention has high availability as a therapeutic agent for known harmful strains and excellent antibacterial activity.

< Antifungal activity assay >

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

Next, a sterilized underlay consisting of citrate phosphate buffer (9 mM sodium phosphate, 1 mM sodium citrate, pH7.4), 1% (w/v) type I (low electroendosmosis) agarose, and 0.03% TSB Cultured bacteria (4 × 10 ⁶ colony forming units/ml) are added to the gel (underlay gel), mixed, poured into a square plate, and when the underlay gel is hardened, a hole with a diameter of 3 mm is made and divided according to concentration (0, 12.5 , 25, 50, 100 and 200 μg/ml), and 5 μl of the peptide (Proteiamycin-5) was put into the hole.

After incubation at 37 ° C. for 3 hours to diffuse the peptide, 10 ml of overlay gel (6% TSB, 1% agarose) was poured and incubated again at 37 ° C. to measure the diameter of the clear zone. shown in Figure 1.

As shown in FIG. 1, the peptide proteiamycin-5 exhibited antifungal activity against Candida albicans, and the antifungal activity increased in a concentration-dependent manner. Through this, it was confirmed that the peptide proteiamycin-5 according to the present invention has excellent antifungal activity.

Through this, it was confirmed that the peptide protethiamycin-5 according to the present invention exhibits a wide range of excellent antibacterial and antifungal activities.

< test example 2. Cytotoxicity test>

A hemolysis assay was performed to investigate the cytotoxicity of the proteiamycin-5 peptide. After washing mouse erythrocytes three times with phosphate-sodium chloride buffer, pH=7.4 (PBS), the cells were diluted with phosphate-sodium chloride buffer to prepare a 5.00% red blood cell solution. Next, 100 μl of the 5.0% red blood cell solution was dispensed into tubes, and proteiamycin-5 was treated for 24 hours at different concentrations (0, 12.5, 25, 50, 100 and 200 μg/ml). 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, the supernatant was centrifuged for 10 minutes at a rotational speed of 1000 rpm in a centrifuge, and the supernatant was transferred to a 96-well culture vessel, and then confirmed by measuring absorbance 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% disruptive capacity, and the value when only red blood cells were added was calculated as 0% disruptive capacity. At this time, the destructive power of the peptide was calculated by the following equation.

[Equation 1]

% destructive activity = (absorbance of solution treated with peptide 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 proteiamycin-5 showed insignificant ability to destroy red blood cells even when treated at a high concentration of 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 proteiamycin-5 according to the present invention has minimal cytotoxicity, so it can be used as a safe antibacterial, antifungal and antibiotic, as well as a food or feed preservative, and cosmetics or pharmaceuticals. It is confirmed that it can be applied usefully did

<110> REPUBLIC OF KOREA(MANAGEMENT : RURAL DEVELOPMENT ADMINISTRATION) <120> A protaetiamycine 5 peptide isolated from Portaetia brevitarsis seulensis larva and A use of the peptide <130> NSH1-155 <160> 1 <170> KoPatentIn 3.0 <210> 1 <211> 15 <212> PRT <213> artificial sequence <220> <223> Protaetia brevitarsis seulensis <400> 1 Trp Val Ile Ile Leu Ala Lys Gln Thr Lys Ile Val Lys Ile Lys 1 5 10 15

Claims (12)

Peptide represented by SEQ ID NO: 1:
SEQ ID NO: 1: WVIILAKQTKIVKIK-NH ₂ According to claim 1,
Wherein the peptide exhibits antibacterial or antifungal activity. According to claim 1,
The peptide is Escherichia coli , Pseudomonas aeruginosa , Staphylococcus aureus , Klebsiella pneumoniae , Bacillus subtilis , Vibrio parahaemolyticus , Propionibacter Showing antibacterial or antifungal activity against any one or more selected from the group consisting of Propionibacterium acnes , Salmonella typhimurium , Shigella flexneri and Candida albicans phosphorus, peptides. An antibacterial or antifungal composition comprising the peptide Protaetiamycin-5 consisting of the amino acid sequence of SEQ ID NO: 1. According to claim 4,
The peptide is Escherichia coli , Pseudomonas aeruginosa , Staphylococcus aureus , Klebsiella pneumoniae , Bacillus subtilis , Vibrio parahaemolyticus , Propionibacter Leeum acnes ( Propionibacterium acnes ), rat titus bacteria ( Salmonella typhimurium ) and Shigella flexneri ( Shigella flexneri ) Which exhibits antibacterial activity against at least one selected from the group consisting of, antibacterial or antifungal composition. According to claim 4,
The peptide exhibits antifungal activity against Candida albicans , an antibacterial or antifungal composition. An antibiotic comprising the peptide Protaetiamycin-5 consisting of the amino acid sequence of SEQ ID NO: 1 as an active ingredient. An external skin preparation for antibacterial or antifungal use 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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