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Polypeptide having anti-bacterial and anti-inflammatory activity and application thereof

A peptide sequence, bacterial technology, applied in the application of skin care products or cosmetics, drugs and external products such as dressings, can solve problems such as weak affinity

Active Publication Date: 2017-04-26
ZHEJIANG UNIV
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

At present, the biological role of brominated tryptophan is still unclear, but the presence of brominated modification can convert the side chain of tryptophan into a substrate with weaker affinity for endogenous proteolytic enzymes, thereby protecting antimicrobial peptides from being Proteolysis, enhancing its antibacterial activity

Method used

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  • Polypeptide having anti-bacterial and anti-inflammatory activity and application thereof
  • Polypeptide having anti-bacterial and anti-inflammatory activity and application thereof
  • Polypeptide having anti-bacterial and anti-inflammatory activity and application thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0029] Embodiment 1: Polypeptide 1 (GW28-Br)

[0030] A polypeptide 1 (GW28-Br) is a small molecule derived from the antimicrobial peptide Centrocin, consisting of 30 amino acid residues and modified by bromination, with a molecular weight of 3321.6Da. GW28-Br is an amphiphilic, α-helical antimicrobial peptide with one polar surface and one nonpolar surface. The nucleotide sequence of the polypeptide 1 (GW28-Br) is shown in SEQ ID NO.1:

[0031] GlyTrp(Br)PheLysLysThrPheHisLysValSerHisAlaValLysSerGlyIleHisAlaGlyGlnArgGlyCysSerAlaLeuGlyPhe.

Embodiment 2

[0032] Embodiment 2: polypeptide derivative

[0033] The amino acid sequences of the six derivatives of the polypeptide 1 (GW28-Br) are as follows:

[0034] SEQ ID NO.2: GlyTrp(Br)PheLysLysThrPheHisLysValSerHisAlaValLysSerGlyIleHisAla;

[0035] SEQ ID NO. 3: SerTrp(Br)PheSerArgThrValHisAsnValGlyAsnAlaValArgLysGlyIleHisAlaGlyGlnGlyValCysSerGlyLeuGlyLeu;

[0036]SEQ ID NO.4:

[0037] GlyTrp(Br)Trp(Br)ArgArgThrValAspLysValArgAsnAlaGlyArgLysValAlaGlyPheAlaSerLysAlaCysGlyAlaLeuGlyHis;

[0038] SEQ ID NO.5: GlyTrp(Br)Trp(Br)ArgArgThrValAspLysValArgAsnAlaGlyArgLysValAla;

[0039] SEQ ID NO.6:

[0040] Trp(Br)GlyHisLysLeuArgSerSerTrp(Br)AsnLysValLysHisAlaValLysLysGlyAlaGlyTyrAlaSerGlyAlaCysArgValLeuGlyHis;

[0041] SEQ ID NO. 7: Trp(Br)GlyHisLysLeuArgSerSerTrp(Br)AsnLysValLysHisAlaValLysLys.

[0042] A further derivative is a derivative produced by the substitution of an amino acid residue in the above polypeptide 1 (SEQ ID NO.1) or polypeptide derivatives (SEQ ID NO.2-7), or th...

Embodiment 3

[0043] Embodiment 3: GW28-Br in vitro antibacterial activity evaluation

[0044] The Corynebacterium acnes isolated from the skin lesions of 15 acne patients were clinically collected, and the MIC values ​​(minimum inhibitory concentration) of GW28-Br and clindamycin against clinical isolates and ATCC strains were detected by micro broth method. The results are shown in Table 1. GW28-Br has obvious inhibitory effect on clinically isolated Corynebacterium acnes, including 6 clindamycin-resistant strains. The average MIC value of GW28-Br was 11.8 mg / L, which was significantly lower than the MIC value of 31.2 mg / L of clindamycin against 9 clinical strains of Corynebacterium acnes (P<0.05). GW28-Br can also inhibit Staphylococcus aureus ATCC 25913 (MIC value 32 mg / L) and Staphylococcus epidermidis ATCC 12228 (MIC value 16 mg / L) commonly found in acne lesions, while clindamycin can only inhibit Staphylococcus epidermidis ATCC12228 (MIC value 64mg / L).

[0045] Table 1 MIC value (m...

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Abstract

The invention provides a polypeptide having the molecular weight of 3321.6 Da and having an amino acid sequence as shown in SEQ ID NO.1. The invention also provides six derivatives of the polypeptide. The polypeptide and the derivatives thereof provided by the invention have efficient broad-spectrum bacteriostatic effect on gram positive bacteria and gram negative bacteria (especially having good killing effect on anti-clindamycin anaerobic propionibacterium acnes), fungi and yeasts, and have high activity (the concentration for killing the propionibacterium acnes in vitro can be only 0.125 mg / L). The polypeptide and the derivatives thereof can be applied in preparation of microbial bacterial and fungal infection-controlling and anti-inflammatory products, wherein the products include externally-applied disinfectants, anti-bacterial agents, wound-protection or infection-prevention dressings, acne treating drugs, skin care products, cosmetics and the like. The polypeptide is designed and synthesized based on a tryptophan bromide-containing fragment of a marine biological sea urchin, has stronger bacteria inhibiting or killing and anti-inflammatory effects and better stability, and can be used as an antibiotic substitute.

Description

technical field [0001] The invention belongs to the field of biological technology, and relates to a polypeptide with antibacterial and anti-inflammatory activities, and its application in the preparation of medicines and external products containing the polypeptide, such as dressings, skin care products or cosmetics. Background technique [0002] Antimicrobial peptides are a class of small molecular defense polypeptides synthesized by organisms and are important members of the animal's innate immune system. In 1972, Swedish scientist Boman and others first discovered antimicrobial peptides and their immune functions in fruit ropes. Subsequently, many researchers successively discovered and isolated thousands of peptides from bacteria, fungi, higher plants, invertebrates, vertebrates and even humans. Peptides with antibacterial activity. [0003] The bacteriostatic mechanism of antimicrobial peptides includes barrel stave model, carpet model and toroidal pore model. Insert...

Claims

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Application Information

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IPC IPC(8): C07K14/435A61K38/17A61P31/04A61P31/10A61P17/10A61K8/64A61Q19/00A61L15/32A61L15/46
CPCA61K8/64A61K38/00A61L15/32A61L15/46A61Q19/00C07K14/43504
Inventor 程浩韩睿朱可建
Owner ZHEJIANG UNIV
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