KR102038487B1 - Antimicrobial or antifungal composition comprising telomerase peptide - Google Patents
Antimicrobial or antifungal composition comprising telomerase peptide Download PDFInfo
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- KR102038487B1 KR102038487B1 KR1020120104178A KR20120104178A KR102038487B1 KR 102038487 B1 KR102038487 B1 KR 102038487B1 KR 1020120104178 A KR1020120104178 A KR 1020120104178A KR 20120104178 A KR20120104178 A KR 20120104178A KR 102038487 B1 KR102038487 B1 KR 102038487B1
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Abstract
The present invention discloses an antimicrobial or antifungal composition comprising as an active ingredient a peptide having a sequence of SEQ ID NO: 1, a peptide which is a fragment of the sequence of SEQ ID NO: 1, or a peptide having a sequence homology of 80% or more with the peptide sequence.
Description
The present invention relates to a composition comprising a telomerase peptide having antimicrobial activity.
Telomere is a genetic material repeatedly present at the end of a chromosome and is known to prevent damage to the chromosome or binding to another chromosome. Each time a cell divides, the telomeres become slightly shorter. After a certain number of cell divisions, the telomeres become very short, and the cells stop dividing and die. On the other hand, elongation of telomeres is known to prolong cell life. For example, cancer cells secrete an enzyme called telomerase, which prevents telomeres from shortening, so that cancer cells can continue to proliferate without dying.
The present invention seeks to provide compositions having excellent antimicrobial or antifungal activity, including peptides.
One aspect of the present invention is an antimicrobial or antifungal composition comprising a peptide having a sequence of SEQ ID NO: 1, a peptide that is a fragment of SEQ ID NO: 1, or a peptide having a sequence homology of 80% or more with the peptide sequence as an active ingredient. To provide.
Since the peptide having the sequence of SEQ ID NO: 1, the peptide which is a fragment of the sequence of SEQ ID NO: 1, or the peptide having a sequence homology of 80% or more with the peptide sequence has an excellent fungicidal inhibitory effect, the composition comprising the antimicrobial or antifungal Can be used for In addition, a peptide having a sequence of SEQ ID NO: 1, a peptide that is a fragment of SEQ ID NO: 1, or a peptide having a sequence homology of 80% or more with the peptide sequence according to an aspect of the present invention has low cellular toxicity and low in vivo stability. As it is high, it can be usefully utilized.
1 is a graph showing the antimicrobial activity of E. coli of
Figure 2 is a graph showing the antimicrobial activity of E. floccosum of
3 is a graph showing the antimicrobial activity against T. mentargophytes of
Nearly all higher organisms are known to accumulate or secrete the body's immune system and antibacterial peptides as a defense against pathogenic microbes. To date, more than 2,000 antimicrobial peptides have been discovered, and these peptides are known to have similar amino acid mechanisms although their amino acid composition differs for each species found.
The mechanism of action of antimicrobial peptides exhibits antimicrobial activity is largely classified into two types.
First, antimicrobial peptides exhibit antimicrobial activity through mechanisms that increase the permeability of cell membranes of bacteria to destroy membrane potential and stop cell metabolism. Most known antimicrobial peptides are known to exhibit this mechanism of action.
Second, the antimicrobial peptide may exhibit antimicrobial activity through the mechanism of action that penetrates into fungal cells and binds to DNA or RNA to inhibit transcription or translation. Such a mechanism is a very powerful mechanism of action. Peptides having such a mechanism of action have a strong antimicrobial effect. However, at present, there is almost no research on peptides having such a mechanism of action.
The antimicrobial peptides, first, have a strong antimicrobial activity against a wide range of microorganisms, second, the host cell acts as an antibiotic that is harmless to the human body by acting only on pathogens invading from the outside without destroying, and third, when inducing resistance of microorganisms is a problem Since it exhibits antimicrobial activity with an activity mechanism completely different from conventional antibiotics, it is less likely to cause resistance. Fourth, since there is no secondary modification such as glycosylation, it can be mass-produced through genetic manipulation. Fifthly, since it has strong physicochemical stability such as heat, acid, or alkali, it has an advantage of great industrial utility in the pharmaceutical and food fields.
One aspect of the invention provides an antimicrobial peptide of a peptide having a sequence of SEQ ID NO: 1, a peptide that is a fragment of SEQ ID NO: 1 or a peptide having at least 80% sequence homology with the peptide sequence. Peptides having the sequence of SEQ ID NO: 1, peptides which are fragments of the sequence of SEQ ID NO: 1, or peptides having at least 80% sequence homology with the peptide sequence can penetrate into fungal cells and bind to DNA or RNA to transcription or translation. It exhibits antimicrobial activity through a mechanism of action that inhibits translation.
An aspect of the present invention provides an antimicrobial or antifungal composition comprising a peptide having a sequence of SEQ ID NO: 1, a peptide that is a fragment of SEQ ID NO: 1, or a peptide having a sequence homology of 80% or more with the peptide sequence as an active ingredient. to provide.
Peptides disclosed herein can include peptides having a sequence of SEQ ID NO: 1 or a peptide that is a fragment of sequence of SEQ ID NO: 1 and a peptide having at least 80%, at least 85%, at least 90%, or at least 95% sequence homology. Can be. In addition, the peptides disclosed herein may include peptides comprising any one of SEQ ID NOs: 1 to 56, and peptides that differ from one or more amino acids, two or more amino acids, three or more amino acids, four or more amino acids. .
Peptides disclosed herein can be wild-type peptides identified and isolated from a natural source. On the other hand, a peptide disclosed herein is an artificial variant, comprising an amino acid sequence in which one or more amino acids are substituted, deleted, and / or inserted as compared to a peptide having a sequence of SEQ ID NO: 1 or a peptide that is a fragment of the sequence of SEQ ID NO: 1 Can be. Amino acid changes in the wild type polypeptide as well as in artificial variants include conservative amino acid substitutions that do not significantly affect the folding and / or activity of the protein. Examples of conservative substitutions include basic amino acids (arginine, lysine and histidine), acidic amino acids (glutamic acid and aspartic acid), polar amino acids (glutamine and asparagine), hydrophobic amino acids (leucine, isoleucine, valine and methionine), aromatic amino acids (phenylalanine, Tryptophan and tyrosine), and small amino acids (glycine, alanine, serine and threonine). Amino acid substitutions that generally do not alter specific activity are known in the art. The most common exchanges are Ala / Ser, Val / Ile, Asp / Glu, Thr / Ser, Ala / Gly, Ala / Thr, Ser / Asn, Ala / Val, Ser / Gly, Tyr / Phe, Ala / Pro, Lys / Arg, Asp / Asn, Leu / Ile, Leu / Val, Ala / Glu, and Asp / Gly, and vice versa.
In one aspect of the invention, amino acid changes belong to the property that allows the physicochemical properties of the peptide to be altered. For example, amino acid changes can be made, such as improving the thermal stability of the peptide, altering substrate specificity, changing the optimal pH, and the like.
In one aspect of the invention, a peptide having a sequence of SEQ ID NO: 1, a peptide that is a fragment of the sequence of SEQ ID NO: 1, or a peptide having at least 80% sequence homology with the peptide sequence may consist of up to 30 amino acids. have. In another aspect of the present invention, a peptide having a sequence of SEQ ID NO: 1, a peptide that is a fragment of SEQ ID NO: 1, or a peptide having 80% or more sequence homology with the peptide sequence may be any one of SEQ ID NOs: 2 to 56 It may be a peptide comprising a sequence or a sequence having at least 80% sequence homology with the sequence. In another aspect of the present invention, a peptide having a sequence of SEQ ID NO: 1, a peptide that is a fragment of SEQ ID NO: 1, or a peptide having 80% or more sequence homology with the peptide sequence may be any one of SEQ ID NOs: 2 to 56 Sequence or sequence having 80% or more sequence homology with said sequence.
In one aspect of the invention, a peptide having a sequence of SEQ ID NO: 1, a peptide that is a fragment of the sequence of SEQ ID NO: 1, or a peptide having at least 80% sequence homology with the peptide sequence is a telomerase, specifically human ( Homo sapiens). ) Peptides derived from telomerase.
The peptides set forth in SEQ ID NOs: 1 to 56 are shown in Tables 1 and 2 below. The "names" in Tables 1 and 2 below are named to distinguish each peptide. In one aspect of the invention, the peptide set forth in SEQ ID NO: 1 represents the entire peptide of human telomerase. In another aspect of the present invention, at least one of the peptides set forth in SEQ ID NOS: 1 to 56 includes a "synthetic peptide" synthesized by selecting and synthesizing a peptide at that position among the peptides contained in telomerase.
GAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQVWKNPTFFLRVISDTASLCYSILKAKNAGMSLGAKGAAGPLPSEAVQWLCHQAFLLKLTRHRVTYVPLLGSLRTAQTQLSRKLPGT TLTALEAAANPALPSDFKTILD
One aspect of the present invention is an antimicrobial or antifungal pharmaceutical composition comprising a peptide having a sequence of SEQ ID NO: 1, a peptide that is a fragment of SEQ ID NO: 1, or a peptide having a sequence homology of 80% or more with the peptide sequence as an active ingredient. To provide. The pharmaceutical composition according to an aspect of the present invention comprises a peptide having a sequence of SEQ ID NO: 1, a peptide that is a fragment of SEQ ID NO: 1, or a peptide having a sequence homology of 80% or more with the peptide sequence as an active ingredient, and has excellent antibacterial activity. Since it has an antifungal effect, it is possible to prevent or treat various diseases and symptoms caused by pathogens.
One aspect of the present invention provides antimicrobial and antifungal use of a peptide having a sequence of SEQ ID NO: 1, a peptide that is a fragment of SEQ ID NO: 1, or a peptide having at least 80% sequence homology with the peptide sequence.
One aspect of the invention provides a method of applying to a subject a peptide having a sequence of SEQ ID NO: 1, a peptide that is a fragment of SEQ ID NO: 1, or a peptide having at least 80% sequence homology with the peptide sequence, or a composition comprising the same. Provided are methods for preventing or treating a pathogen infection.
One aspect of the invention provides a peptide comprising a peptide having a sequence of SEQ ID NO: 1, a peptide that is a fragment of the sequence of SEQ ID NO: 1 or a peptide having at least 80% sequence homology with the peptide sequence; And instructions for disclosing one or more of the dosage, route of administration, frequency of administration, and indications of the peptide or composition comprising the same.
An aspect of the present invention provides an antibacterial or antifungal skin external preparation comprising as an active ingredient a peptide having a sequence of SEQ ID NO: 1, a peptide that is a fragment of SEQ ID NO: 1, or a peptide having a sequence homology of 80% or more with the peptide sequence. , Or a cosmetic composition.
An aspect of the present invention is an antimicrobial or antifungal food composition comprising a peptide having a sequence of SEQ ID NO: 1, a peptide which is a fragment of SEQ ID NO: 1, or a peptide having a sequence homology of 80% or more with the peptide sequence as an active ingredient. To provide.
As used herein, "antibacterial activity" is defined as activity that can kill microbial cells or inhibit their growth. In the context of the present invention, "antibacterial" means that there is a bactericidal and / or bacteriostatic and / or fungicidal and / or bacteriostatic effect. "Sterilization" means the killing of bacteria, fungi, or cells of lower eukaryotes, such as yeasts or algae, protozoa, etc., and "fungal bacteria" means lower eukaryotes, protists, such as bacteria, yeast, or It means that it is possible to inhibit the growth of fungi, that is, the growth of lower eukaryotes, protists or fungal cells such as bacteria and yeasts. By "fungicidal" is meant that it can kill fungal cells. The term "fungal fungus" means that it is possible to inhibit fungal growth, ie growth of fungal cells. The term "microbial cell" is a broad concept including bacteria, fungi, or lower eukaryotes or protists such as yeast or algae.
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The antimicrobial and antifungal peptides disclosed herein are applicable to a wide range of applications regardless of the type of microorganism or the antimicrobial target. Typically useful at any site contaminated by bacteria, fungi, yeast or algae. Typically, antibacterial objects are aqueous systems such as cooling water systems, laundry rinsing water, oil systems such as cutting oils, lubricants, oil fields, and the like, and are places where it is necessary to kill microorganisms or inhibit their growth. In addition, the antimicrobial, antifungal peptides disclosed herein can be used in all applications where antimicrobial, antifungal compositions are known to be useful, such as wood, latex, adhesives, glue, paper, cardboard, textiles, leather, plastics, caulking, and feed protection. Can be.
Other uses include preservation of foods, beverages, cosmetics such as lotions, creams, gels, ointments, soaps, shampoos, conditioners, limiting agents, deodorants, toothpastes, contact lens products, enzyme preparations, or food ingredients.
On the other hand, the peptides disclosed herein are antiseptics, for example in the treatment of acne, eye or mouth infections, skin infections; In limiting or deodorizing agents; In salts for foot baths; It is useful for cleaning and disinfecting contact lenses, hard surfaces, teeth (oral care), wounds and bruises.
In addition, one aspect of the invention relates to the use of an antimicrobial peptide or composition as a medicament. Further, the peptides or compositions described herein may also be medicament for controlling or fighting microorganisms, such as bacteria, fungi, or lower eukaryotes, such as yeast or algae, protozoa, including gram positive or gram negative It can be used for the preparation of. In particular, microbial infections include, but are not limited to, infectious skin diseases such as acne or athlete's foot; Lung diseases, including but not limited to tuberculosis and cystic fibrosis; It may be related to sexually transmitted diseases including but not limited to gonorrhea and chlamydia.
The composition according to one aspect of the present invention comprises 0.1 μg / mg to 1 mg / of a peptide having a sequence of SEQ ID NO: 1, a peptide that is a fragment of sequence of SEQ ID NO: 1, or a peptide having at least 80% sequence homology with the peptide sequence. Mg, specifically 1 μg / mg to 0.5 mg / mg, more specifically 10 μg / mg to 0.1 mg / mg. When included in the above range is not only suitable for showing the intended effect of the present invention, it can satisfy both the stability and safety of the composition, it may be appropriate to include in the above range in terms of cost-effectiveness.
The composition according to one aspect of the present invention can be applied to all animals including humans, dogs, chickens, pigs, cattle, sheep, guinea pigs or monkeys.
The pharmaceutical composition according to one aspect of the present invention may be administered orally, rectal, transdermal, intravenous, intramuscular, intraperitoneal, intramedullary, intradural or subcutaneous.
Formulations for oral administration may be, but are not limited to, tablets, pills, soft or hard capsules, granules, powders, solutions or emulsions. Formulations for parenteral administration may be, but are not limited to, injections, drops, lotions, ointments, gels, creams, suspensions, emulsions, suppositories, patches or sprays.
Pharmaceutical compositions according to one aspect of the invention may include additives such as diluents, excipients, lubricants, binders, disintegrants, buffers, dispersants, surfactants, colorants, flavoring or sweetening agents as needed. Pharmaceutical compositions according to one aspect of the invention may be prepared by conventional methods in the art.
The active ingredient of the pharmaceutical composition according to one aspect of the present invention will vary depending on the age, sex, weight, pathology and severity of the subject to be administered, the route of administration or the judgment of the prescriber. Dosage determination based on these factors is within the level of ordinary skill in the art and its daily dosage may be, for example, 0.1 μg / kg / day to 1 g / kg / day, specifically 1 μg / kg / day to 10 mg / kg Per day, more specifically 10 μg / kg / day to 1 mg / kg / day, and more specifically 50 μg / kg / day to 100 μg / kg / day, but is not limited thereto. The pharmaceutical composition according to one aspect of the present invention may be administered once to three times a day, but is not limited thereto.
Cosmetic compositions according to one aspect of the invention may be provided in all formulations suitable for topical application. For example, it may be provided in the form of a solution, an emulsion obtained by dispersing an oil phase in an aqueous phase, an emulsion obtained by dispersing an aqueous phase in an oil phase, a suspension, a solid, a gel, a powder, a paste, a foam, or an aerosol. Such formulations may be prepared according to conventional methods in the art.
The cosmetic composition according to one aspect of the present invention may include other ingredients that can give a synergistic effect to the main effect, preferably within the range of not impairing the main effect. In addition, the cosmetic composition according to an aspect of the present invention may further include a moisturizer, an emulsifier, a surfactant, a UV absorber, a preservative, a bactericide, an antioxidant, a pH adjuster, an organic or inorganic pigment, a perfume, a cooling agent, or a restriction agent. It may include. The blending amount of the above components can be easily selected by those skilled in the art within the range that does not impair the object and effect of the present invention, the blending amount is 0.01 to 5% by weight, specifically 0.01 to 3% by weight based on the total weight of the cosmetic composition Can be.
The formulation of the food composition according to one aspect of the present invention is not particularly limited, but may be, for example, formulated into tablets, granules, powders, solutions, solid preparations, and the like. Each formulation may be appropriately selected and formulated by those skilled in the art according to the formulation or purpose of use, in addition to the active ingredient, and may be synergistic when applied simultaneously with other raw materials.
Determination of the dosage of the active ingredient is within the level of those skilled in the art, the daily dosage of which is for example specifically 1 μg / kg / day to 10 mg / kg / day, more specifically 10 μg / kg / day To 1 mg / kg / day, and more specifically, 50 μg / kg / day to 100 μg / kg / day, but is not limited thereto, and various factors such as age, health condition, and complications of the subject to be administered. It may vary.
Hereinafter, the configuration and effects of the present invention will be described in more detail with reference to experimental examples. However, the following experimental examples are provided only for the purpose of illustration in order to help the understanding of the present invention, and the scope and scope of the present invention are not limited thereto.
Experimental Example Evaluation of Antimicrobial Activity of Peptides
To 1 ml of liquid medium was added
As can be seen from the above results,
SEQUENCE LISTING <110> KAEL-GemVax Co., Ltd. <120> Composition for antimicrobial or antivirus comprising telomerase peptide <130> 12P554 <160> 56 <170> PatentIn version 3.2 <210> 1 <211> 1132 <212> PRT <213> Homo sapiens <400> 1 Met Pro Arg Ala Pro Arg Cys Arg Ala Val Arg Ser Leu Leu Arg Ser 1 5 10 15 His Tyr Arg Glu Val Leu Pro Leu Ala Thr Phe Val Arg Arg Leu Gly 20 25 30 Pro Gln Gly Trp Arg Leu Val Gln Arg Gly Asp Pro Ala Ala Phe Arg 35 40 45 Ala Leu Val Ala Gln Cys Leu Val Cys Val Pro Trp Asp Ala Arg Pro 50 55 60 Pro Pro Ala Ala Pro Ser Phe Arg Gln Val Ser Cys Leu Lys Glu Leu 65 70 75 80 Val Ala Arg Val Leu Gln Arg Leu Cys Glu Arg Gly Ala Lys Asn Val 85 90 95 Leu Ala Phe Gly Phe Ala Leu Leu Asp Gly Ala Arg Gly Gly Pro Pro 100 105 110 Glu Ala Phe Thr Thr Ser Ser Val Arg Ser Tyr Leu Pro Asn Thr Val Thr 115 120 125 Asp Ala Leu Arg Gly Ser Gly Ala Trp Gly Leu Leu Leu Arg Arg Val 130 135 140 Gly Asp Asp Val Leu Val His Leu Leu Ala Arg Cys Ala Leu Phe Val 145 150 155 160 Leu Val Ala Pro Ser Cys Ala Tyr Gln Val Cys Gly Pro Pro Leu Tyr 165 170 175 Gln Leu Gly Ala Ala Thr Gln Ala Arg Pro Pro Pro His Ala Ser Gly 180 185 190 Pro Arg Arg Arg Leu Gly Cys Glu Arg Ala Trp Asn His Ser Val Arg 195 200 205 Glu Ala Gly Val Pro Leu Gly Leu Pro Ala Pro Gly Ala Arg Arg Arg 210 215 220 Gly Gly Ser Ala Ser Arg Ser Leu Pro Leu Pro Lys Arg Pro Arg Arg 225 230 235 240 Gly Ala Ala Pro Glu Pro Glu Arg Thr Pro Val Gly Gln Gly Ser Trp 245 250 255 Ala His Pro Gly Arg Thr Arg Gly Pro Ser Asp Arg Gly Phe Cys Val 260 265 270 Val Ser Pro Ala Arg Pro Ala Glu Glu Ala Thr Ser Leu Glu Gly Ala 275 280 285 Leu Ser Gly Thr Arg His Ser His Pro Ser Val Gly Arg Gln His His 290 295 300 Ala Gly Pro Pro Ser Thr Ser Arg Pro Pro Arg Pro Trp Asp Thr Pro 305 310 315 320 Cys Pro Pro Val Tyr Ala Glu Thr Lys His Phe Leu Tyr Ser Ser Gly 325 330 335 Asp Lys Glu Gln Leu Arg Pro Ser Phe Leu Leu Ser Ser Leu Arg Pro 340 345 350 Ser Leu Thr Gly Ala Arg Arg Leu Val Glu Thr Ile Phe Leu Gly Ser 355 360 365 Arg Pro Trp Met Pro Gly Thr Pro Arg Arg Leu Pro Arg Leu Pro Gln 370 375 380 Arg Tyr Trp Gln Met Arg Pro Leu Phe Leu Glu Leu Leu Gly Asn His 385 390 395 400 Ala Gln Cys Pro Tyr Gly Val Leu Leu Lys Thr His Cys Pro Leu Arg 405 410 415 Ala Ala Val Thr Pro Ala Ala Gly Val Cys Ala Arg Glu Lys Pro Gln 420 425 430 Gly Ser Val Ala Ala Pro Glu Glu Glu Asp Thr Asp Pro Arg Arg Leu 435 440 445 Val Gln Leu Leu Arg Gln His Ser Ser Pro Trp Gln Val Tyr Gly Phe 450 455 460 Val Arg Ala Cys Leu Arg Arg Leu Val Pro Pro Gly Leu Trp Gly Ser 465 470 475 480 Arg His Asn Glu Arg Arg Phe Leu Arg Asn Thr Lys Lys Phe Ile Ser 485 490 495 Leu Gly Lys His Ala Lys Leu Ser Leu Gln Glu Leu Thr Trp Lys Met 500 505 510 Ser Val Arg Asp Cys Ala Trp Leu Arg Arg Ser Pro Gly Val Gly Cys 515 520 525 Val Pro Ala Ala Glu His Arg Leu Arg Glu Glu Ile Leu Ala Lys Phe 530 535 540 Leu His Trp Leu Met Ser Val Tyr Val Val Glu Leu Leu Arg Ser Phe 545 550 555 560 Phe Tyr Val Thr Glu Thr Thr Phe Gln Lys Asn Arg Leu Phe Phe Tyr 565 570 575 Arg Lys Ser Val Trp Ser Lys Leu Gln Ser Ile Gly Ile Arg Gln His 580 585 590 Leu Lys Arg Val Gln Leu Arg Glu Leu Ser Glu Ala Glu Val Arg Gln 595 600 605 His Arg Glu Ala Arg Pro Ala Leu Leu Thr Ser Arg Leu Arg Phe Ile 610 615 620 Pro Lys Pro Asp Gly Leu Arg Pro Ile Val Asn Met Asp Tyr Val Val 625 630 635 640 Gly Ala Arg Thr Phe Arg Arg Glu Lys Arg Ala Glu Arg Leu Thr Ser 645 650 655 Arg Val Lys Ala Leu Phe Ser Val Leu Asn Tyr Glu Arg Ala Arg Arg 660 665 670 Pro Gly Leu Leu Gly Ala Ser Val Leu Gly Leu Asp Asp Ile His Arg 675 680 685 Ala Trp Arg Thr Phe Val Leu Arg Val Arg Ala Gln Asp Pro Pro Pro 690 695 700 Glu Leu Tyr Phe Val Lys Val Asp Val Thr Gly Ala Tyr Asp Thr Ile 705 710 715 720 Pro Gln Asp Arg Leu Thr Glu Val Ile Ala Ser Ile Ile Lys Pro Gln 725 730 735 Asn Thr Tyr Cys Val Arg Arg Tyr Ala Val Val Gln Lys Ala Ala His 740 745 750 Gly His Val Arg Lys Ala Phe Lys Ser His Val Ser Thr Leu Thr Asp 755 760 765 Leu Gln Pro Tyr Met Arg Gln Phe Val Ala His Leu Gln Glu Thr Ser 770 775 780 Pro Leu Arg Asp Ala Val Val Ile Glu Gln Ser Ser Ser Leu Asn Glu 785 790 795 800 Ala Ser Ser Gly Leu Phe Asp Val Phe Leu Arg Phe Met Cys His His 805 810 815 Ala Val Arg Ile Arg Gly Lys Ser Tyr Val Gln Cys Gln Gly Ile Pro 820 825 830 Gln Gly Ser Ile Leu Ser Thr Leu Leu Cys Ser Leu Cys Tyr Gly Asp 835 840 845 Met Glu Asn Lys Leu Phe Ala Gly Ile Arg Arg Asp Gly Leu Leu Leu 850 855 860 Arg Leu Val Asp Asp Phe Leu Leu Val Thr Pro His Leu Thr His Ala 865 870 875 880 Lys Thr Phe Leu Arg Thr Leu Val Arg Gly Val Pro Glu Tyr Gly Cys 885 890 895 Val Val Asn Leu Arg Lys Thr Val Val Asn Phe Pro Val Glu Asp Glu 900 905 910 Ala Leu Gly Gly Thr Ala Phe Val Gln Met Pro Ala His Gly Leu Phe 915 920 925 Pro Trp Cys Gly Leu Leu Leu Asp Thr Arg Thr Leu Glu Val Gln Ser 930 935 940 Asp Tyr Ser Ser Tyr Ala Arg Thr Ser Ile Arg Ala Ser Leu Thr Phe 945 950 955 960 Asn Arg Gly Phe Lys Ala Gly Arg Asn Met Arg Arg Lys Leu Phe Gly 965 970 975 Val Leu Arg Leu Lys Cys His Ser Leu Phe Leu Asp Leu Gln Val Asn 980 985 990 Ser Leu Gln Thr Val Cys Thr Asn Ile Tyr Lys Ile Leu Leu Leu Gln 995 1000 1005 Ala Tyr Arg Phe His Ala Cys Val Leu Gln Leu Pro Phe His Gln 1010 1015 1020 Gln Val Trp Lys Asn Pro Thr Phe Phe Leu Arg Val Ile Ser Asp 1025 1030 1035 Thr Ala Ser Leu Cys Tyr Ser Ile Leu Lys Ala Lys Asn Ala Gly 1040 1045 1050 Met Ser Leu Gly Ala Lys Gly Ala Ala Gly Pro Leu Pro Ser Glu 1055 1060 1065 Ala Val Gln Trp Leu Cys His Gln Ala Phe Leu Leu Lys Leu Thr 1070 1075 1080 Arg His Arg Val Thr Tyr Val Pro Leu Leu Gly Ser Leu Arg Thr 1085 1090 1095 Ala Gln Thr Gln Leu Ser Arg Lys Leu Pro Gly Thr Thr Leu Thr 1100 1105 1110 Ala Leu Glu Ala Ala Ala Asn Pro Ala Leu Pro Ser Asp Phe Lys 1115 1120 1125 Thr Ile Leu Asp 1130 <210> 2 <211> 16 <212> PRT <213> Homo sapiens <400> 2 Glu Ala Arg Pro Ala Leu Leu Thr Ser Arg Leu Arg Phe Ile Pro Lys 1 5 10 15 <210> 3 <211> 30 <212> PRT <213> Homo sapiens <400> 3 Ala Leu Phe Ser Val Leu Asn Tyr Glu Arg Ala Arg Arg Pro Gly Leu 1 5 10 15 Leu Gly Ala Ser Val Leu Gly Leu Asp Asp Ile His Arg Ala 20 25 30 <210> 4 <211> 15 <212> PRT <213> Homo sapiens <400> 4 Ser Val Leu Asn Tyr Glu Arg Ala Arg Arg Pro Gly Leu Leu Gly 1 5 10 15 <210> 5 <211> 10 <212> PRT <213> Homo sapiens <400> 5 Gly Leu Leu Gly Ala Ser Val Leu Gly Leu 1 5 10 <210> 6 <211> 10 <212> PRT <213> Homo sapiens <400> 6 Ala Leu Leu Thr Ser Arg Leu Arg Phe Ile 1 5 10 <210> 7 <211> 9 <212> PRT <213> Homo sapiens <400> 7 Arg Pro Ala Leu Leu Thr Ser Arg Leu 1 5 <210> 8 <211> 9 <212> PRT <213> Homo sapiens <400> 8 Arg Leu Thr Ser Arg Val Lys Ala Leu 1 5 <210> 9 <211> 15 <212> PRT <213> Homo sapiens <400> 9 Arg Thr Phe Val Leu Arg Val Arg Ala Gln Asp Pro Pro Pro Glu 1 5 10 15 <210> 10 <211> 15 <212> PRT <213> Homo sapiens <400> 10 Arg Leu Thr Ser Arg Val Lys Ala Leu Phe Ser Val Leu Asn Tyr 1 5 10 15 <210> 11 <211> 15 <212> PRT <213> Homo sapiens <400> 11 Ala Glu Arg Leu Thr Ser Arg Val Lys Ala Leu Phe Ser Val Leu 1 5 10 15 <210> 12 <211> 9 <212> PRT <213> Homo sapiens <400> 12 Tyr Glu Arg Ala Arg Arg Pro Gly Leu 1 5 <210> 13 <211> 9 <212> PRT <213> Homo sapiens <400> 13 Leu Leu Gly Ala Ser Val Leu Gly Leu 1 5 <210> 14 <211> 10 <212> PRT <213> Homo sapiens <400> 14 Val Leu Gly Leu Asp Asp Ile His Arg Ala 1 5 10 <210> 15 <211> 10 <212> PRT <213> Homo sapiens <400> 15 Gly Ala Ser Val Leu Gly Leu Asp Asp Ile 1 5 10 <210> 16 <211> 10 <212> PRT <213> Homo sapiens <400> 16 Ala Leu Phe Ser Val Leu Asn Tyr Glu Arg 1 5 10 <210> 17 <211> 10 <212> PRT <213> Homo sapiens <400> 17 Ser Val Leu Asn Tyr Glu Arg Ala Arg Arg 1 5 10 <210> 18 <211> 10 <212> PRT <213> Homo sapiens <400> 18 Ser Val Leu Gly Leu Asp Asp Ile His Arg 1 5 10 <210> 19 <211> 10 <212> PRT <213> Homo sapiens <400> 19 Phe Ser Val Leu Asn Tyr Glu Arg Ala Arg 1 5 10 <210> 20 <211> 10 <212> PRT <213> Homo sapiens <400> 20 Asn Tyr Glu Arg Ala Arg Arg Pro Gly Leu 1 5 10 <210> 21 <211> 10 <212> PRT <213> Homo sapiens <400> 21 Tyr Glu Arg Ala Arg Arg Pro Gly Leu Leu 1 5 10 <210> 22 <211> 10 <212> PRT <213> Homo sapiens <400> 22 Arg Pro Gly Leu Leu Gly Ala Ser Val Leu 1 5 10 <210> 23 <211> 9 <212> PRT <213> Homo sapiens <400> 23 Glu Arg Ala Arg Arg Pro Gly Leu Leu 1 5 <210> 24 <211> 9 <212> PRT <213> Homo sapiens <400> 24 Val Leu Gly Leu Asp Asp Ile His Arg 1 5 <210> 25 <211> 9 <212> PRT <213> Homo sapiens <400> 25 Ser Val Leu Asn Tyr Glu Arg Ala Arg 1 5 <210> 26 <211> 9 <212> PRT <213> Homo sapiens <400> 26 Val Leu Asn Tyr Glu Arg Ala Arg Arg 1 5 <210> 27 <211> 9 <212> PRT <213> Homo sapiens <400> 27 Ala Arg Arg Pro Gly Leu Leu Gly Ala 1 5 <210> 28 <211> 9 <212> PRT <213> Homo sapiens <400> 28 Pro Gly Leu Leu Gly Ala Ser Val Leu 1 5 <210> 29 <211> 9 <212> PRT <213> Homo sapiens <400> 29 Arg Arg Pro Gly Leu Leu Gly Ala Ser 1 5 <210> 30 <211> 9 <212> PRT <213> Homo sapiens <400> 30 Ala Leu Phe Ser Val Leu Asn Tyr Glu 1 5 <210> 31 <211> 9 <212> PRT <213> Homo sapiens <400> 31 Gly Leu Leu Gly Ala Ser Val Leu Gly 1 5 <210> 32 <211> 9 <212> PRT <213> Homo sapiens <400> 32 Ser Val Leu Gly Leu Asp Asp Ile His 1 5 <210> 33 <211> 8 <212> PRT <213> Homo sapiens <400> 33 Glu Arg Ala Arg Arg Pro Gly Leu 1 5 <210> 34 <211> 8 <212> PRT <213> Homo sapiens <400> 34 Ala Arg Arg Pro Gly Leu Leu Gly 1 5 <210> 35 <211> 8 <212> PRT <213> Homo sapiens <400> 35 Gly Leu Leu Gly Ala Ser Val Leu 1 5 <210> 36 <211> 8 <212> PRT <213> Homo sapiens <400> 36 Arg Ala Arg Arg Pro Gly Leu Leu 1 5 <210> 37 <211> 8 <212> PRT <213> Homo sapiens <400> 37 Leu Gly Ala Ser Val Leu Gly Leu 1 5 <210> 38 <211> 15 <212> PRT <213> Homo sapiens <400> 38 Val Thr Glu Thr Thr Phe Gln Lys Asn Arg Leu Phe Phe Tyr Arg 1 5 10 15 <210> 39 <211> 15 <212> PRT <213> Homo sapiens <400> 39 Leu Phe Phe Tyr Arg Lys Ser Val Trp Ser Lys Leu Gln Ser Ile 1 5 10 15 <210> 40 <211> 15 <212> PRT <213> Homo sapiens <400> 40 Lys Leu Gln Ser Ile Gly Ile Arg Gln His Leu Lys Arg Val Gln 1 5 10 15 <210> 41 <211> 15 <212> PRT <213> Homo sapiens <400> 41 Glu Ala Glu Val Arg Gln His Arg Glu Ala Arg Pro Ala Leu Leu 1 5 10 15 <210> 42 <211> 15 <212> PRT <213> Homo sapiens <400> 42 Arg Pro Ala Leu Leu Thr Ser Arg Leu Arg Phe Ile Pro Lys Pro 1 5 10 15 <210> 43 <211> 15 <212> PRT <213> Homo sapiens <400> 43 Phe Ile Pro Lys Pro Asp Gly Leu Arg Pro Ile Val Asn Met Asp 1 5 10 15 <210> 44 <211> 15 <212> PRT <213> Homo sapiens <400> 44 Arg Thr Phe Arg Arg Glu Lys Arg Ala Glu Arg Leu Thr Ser Arg 1 5 10 15 <210> 45 <211> 15 <212> PRT <213> Homo sapiens <400> 45 Leu Asp Asp Ile His Arg Ala Trp Arg Thr Phe Val Leu Arg Val 1 5 10 15 <210> 46 <211> 15 <212> PRT <213> Homo sapiens <400> 46 Phe Val Leu Arg Val Arg Ala Gln Asp Pro Pro Pro Glu Leu Tyr 1 5 10 15 <210> 47 <211> 15 <212> PRT <213> Homo sapiens <400> 47 Pro Gln Asp Arg Leu Thr Glu Val Ile Ala Ser Ile Ile Lys Pro 1 5 10 15 <210> 48 <211> 15 <212> PRT <213> Homo sapiens <400> 48 Lys Ser Val Trp Ser Lys Leu Gln Ser Ile Gly Ile Arg Gln His 1 5 10 15 <210> 49 <211> 16 <212> PRT <213> Homo sapiens <400> 49 Leu Lys Arg Val Gln Leu Arg Glu Leu Ser Glu Ala Glu Val Arg Gln 1 5 10 15 <210> 50 <211> 9 <212> PRT <213> Homo sapiens <400> 50 Glu Ala Arg Pro Ala Leu Leu Thr Ser 1 5 <210> 51 <211> 9 <212> PRT <213> Homo sapiens <400> 51 Thr Ser Arg Leu Arg Phe Ile Pro Lys 1 5 <210> 52 <211> 9 <212> PRT <213> Homo sapiens <400> 52 Ala Arg Pro Ala Leu Leu Thr Ser Arg 1 5 <210> 53 <211> 9 <212> PRT <213> Homo sapiens <400> 53 Pro Ala Leu Leu Thr Ser Arg Leu Arg 1 5 <210> 54 <211> 9 <212> PRT <213> Homo sapiens <400> 54 Ala Leu Leu Thr Ser Arg Leu Arg Phe 1 5 <210> 55 <211> 9 <212> PRT <213> Homo sapiens <400> 55 Leu Leu Thr Ser Arg Leu Arg Phe Ile 1 5 <210> 56 <211> 9 <212> PRT <213> Homo sapiens <400> 56 Leu Thr Ser Arg Leu Arg Phe Ile Pro 1 5
Claims (6)
The composition comprises a peptide consisting of the sequence of SEQ ID NO: 2 as an active ingredient,
The bacteria or fungi in E. coli (Escherichia), epi Dermo python in (Epidermophyton) and tricot in python (Trichophyton), comprising at least one bacteria or fungi selected from the group consisting of anti-bacterial or anti-fungal composition.
Peptides are antimicrobial or antifungal compositions derived from human telomerase.
The composition is an antimicrobial or antifungal composition comprising a peptide content of 0.1 μg / mg to 1 mg / mg.
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| Publication number | Priority date | Publication date | Assignee | Title |
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| KR102578891B1 (en) | 2012-05-11 | 2023-09-15 | 주식회사 젬백스앤카엘 | Anti-inflammatory Peptides and Composition comprising the same |
| US10967000B2 (en) | 2012-07-11 | 2021-04-06 | Gemvax & Kael Co., Ltd. | Cell-penetrating peptide, conjugate comprising same and composition comprising same |
| WO2014196841A1 (en) | 2013-06-07 | 2014-12-11 | Kael-Gemvax Co., Ltd. | Biological markers useful in cancer immunotherapy |
| JP6495899B2 (en) | 2013-06-21 | 2019-04-03 | ジェムバックス アンド カエル カンパニー，リミティド | Hormone secretion regulator and composition containing the same |
| KR102694658B1 (en) | 2013-11-22 | 2024-08-14 | 주식회사 젬백스앤카엘 | Peptide having angiogenesis inhibitory activity and composition containing same |
| EP3085380B1 (en) | 2013-12-17 | 2020-06-17 | Gemvax & Kael Co., Ltd. | Composition for treating prostate cancer |
| US10662223B2 (en) | 2014-04-30 | 2020-05-26 | Gemvax & Kael Co., Ltd. | Composition for organ, tissue, or cell transplantation, kit, and transplantation method |
| KR102413243B1 (en) | 2014-12-23 | 2022-06-27 | 주식회사 젬백스앤카엘 | Peptides for treating ophthalmopathy and the Composition Comprising the Same |
| EP3263122B1 (en) | 2015-02-27 | 2020-05-06 | Gemvax & Kael Co., Ltd. | Peptide for preventing hearing loss, and composition comprising same |
| US11015179B2 (en) | 2015-07-02 | 2021-05-25 | Gemvax & Kael Co., Ltd. | Peptide having anti-viral effect and composition containing same |
| JP7114481B2 (en) | 2016-04-07 | 2022-08-08 | ジェムバックス アンド カエル カンパニー，リミティド | Peptides with the efficacy of increasing telomerase activity and lengthening telomeres, and compositions containing the same |
| KR102445492B1 (en) * | 2021-12-24 | 2022-09-21 | 엔케이젠 주식회사 | Composition for mass proliferation of natural killer cells comprising novel peptide, and method for mass proliferation of natural killer cells using the same |
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| EP1783139B8 (en) | 1996-10-01 | 2009-09-23 | Geron Corporation | Human telomerase catalytic subunit |
| US7030211B1 (en) | 1998-07-08 | 2006-04-18 | Gemvax As | Antigenic peptides derived from telomerase |
| KR100441402B1 (en) | 2002-03-26 | 2004-07-23 | 한국과학기술원 | Antimicrobial peptide, its analogs and antimicrobial composition comprising thereof |
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Non-Patent Citations (1)
| Title |
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| Clin. Cancer Res., 2011, 제17권, 제13호, 페이지 4568-4580 |
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