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High cell-selectivity cyclic antimicrobial peptide OIR3 and preparation method and application thereof

An antimicrobial peptide and selective technology, applied in the field of high cell selectivity cyclic antimicrobial peptide OIR3 and its preparation and application

Inactive Publication Date: 2017-05-31
NORTHEAST AGRICULTURAL UNIVERSITY
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

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Problems solved by technology

The second aspect is the production cost issue

Method used

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  • High cell-selectivity cyclic antimicrobial peptide OIR3 and preparation method and application thereof
  • High cell-selectivity cyclic antimicrobial peptide OIR3 and preparation method and application thereof
  • High cell-selectivity cyclic antimicrobial peptide OIR3 and preparation method and application thereof

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Experimental program
Comparison scheme
Effect test

Embodiment 1

[0013] The amino acid sequence of the cyclic antimicrobial peptide OIR1 is:

[0014] Ile Arg Pro Ile Arg Pro

[0015] 1 5 6

[0016] The amino acid sequence of the cyclic antimicrobial peptide OIR2 is:

[0017] Ile Arg Ile Arg Pro Ile Arg Ile Arg Pro

[0018] 1 5 10

[0019] The amino acid sequence of the cyclic antimicrobial peptide OIR3 is:

[0020] Ile Arg Ile Arg Ile Arg Pro Ile Arg Ile Arg Ile Arg Pro

[0021] 1 5 10 14

[0022] Antimicrobial peptides OIR1, OIR2 and OIR3 were designed according to the cyclic peptide template (IleArg)nPro(IleArg)n (n=1, 2 and 3).

Embodiment 2

[0024] The above two antimicrobial peptides were synthesized using a peptide synthesizer. The method was solid-phase chemical synthesis, and the specific steps were:

[0025] 1) The preparation of antimicrobial peptides is carried out one by one from the C-terminus to the N-terminus, and is completed by a peptide synthesizer. First, Fmoc-X (X is the first amino acid at the C-terminal of each antimicrobial peptide) is connected to Pro+2cl2 resin, and then the X-Pro+2cl2 resin is obtained after removing the Fmoc group; then Fmoc-Y-Trt -OH(9-fluorenylmethoxycarboxy-trimethyl-Y, Y is the second amino acid at the C-terminal of each antimicrobial peptide); according to this procedure, it is synthesized from the C-terminus to the N-terminus until the synthesis is completed, and the Fmoc Group side chain protected resin;

[0026] Add cutting reagent to the peptide resin obtained above, react at 20°C for 2 hours in the dark, filter; precipitate TFA (trifluoroacetic acid) for washing, ...

Embodiment 3

[0032] The designed and synthesized antimicrobial peptides were compared and detected by in vitro antibacterial and hemolytic activity tests;

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Abstract

The invention provides a high cell-selectivity cyclic antimicrobial peptide OIR3 and a preparation method and application thereof. The high cell-selectivity cyclic antimicrobial peptide OIR3 has a sequence shown in the formula of SEQ ID No. 1 in the sequence table. The preparation method comprises 1) designing a cyclic antimicrobial peptide OIR3 according to a cyclic antimicrobial peptide template (IleArg)nPro(IleArg)n, wherein n is 3, and 2) synthesizing a peptide resin by a solid phase synthesis method using a polypeptide synthesizer, carrying out TFA cutting to obtain a polypeptide, and carrying out reversed-phase high-performance liquid chromatography purification so that the antimicrobial peptide OIR3 is obtained. The antimicrobial peptide can be used in drugs for treating diseases infected by gram-positive bacteria or gram-negative bacteria. The antimicrobial peptide OIR3 is a high cell-selectivity cyclic antimicrobial peptide, has strong antibacterial activity and weak hemolytic activity, has the highest treatment index and has a great development potential.

Description

technical field [0001] The invention relates to a highly cell-selective circular antimicrobial peptide OIR3 and its preparation method and application. Background technique [0002] Antimicrobial peptides (AMPs), also known as antimicrobial peptides, are a class of small molecule polypeptides produced by specific bacterial genes and have broad-spectrum antibacterial properties. Antimicrobial peptides were first discovered from Hyatophora cecropia in the 1980s. The main biological function of antimicrobial peptides is that they can kill a variety of bacteria including Gram-negative bacteria and Gram-positive bacteria, and have the characteristics of broad antibacterial spectrum and fast sterilization speed. In addition to inhibiting and killing bacteria, it also has antifungal, antiviral, inhibiting or killing tumor cells, killing parasites and antiprotozoa that cause malaria, leishmaniasis and other diseases. Antimicrobial peptides act on the bacterial cell membrane throug...

Claims

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Application Information

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IPC IPC(8): C07K7/64A61K38/12A61P31/04
CPCA61K38/00C07K7/64
Inventor 董娜毕重朋邵长轩单安山
Owner NORTHEAST AGRICULTURAL UNIVERSITY
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