Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Beta hairpin antimicrobial peptide with cross-chain interaction between tryptophan and histidine and preparation method thereof

A technology of histidine cross-chain and interaction, applied in the field of beta hairpin antimicrobial peptides and preparation, can solve the problems of shortened sequence length, high synthesis cost, difficult preparation, etc., and achieves strong inhibitory effect, simple synthesis method, and short sequence length. Effect

Active Publication Date: 2021-12-14
NORTHEAST AGRICULTURAL UNIVERSITY
View PDF0 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0004] Based on the above deficiencies, the present invention provides a β-hairpin antimicrobial peptide with cross-chain interaction between tryptophan and histidine and its preparation method, which can cope with the local acidic pH environment, shorten the sequence length, and solve the difficulty of preparation and synthesis cost. The problem with high disulfide bonds

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Beta hairpin antimicrobial peptide with cross-chain interaction between tryptophan and histidine and preparation method thereof
  • Beta hairpin antimicrobial peptide with cross-chain interaction between tryptophan and histidine and preparation method thereof
  • Beta hairpin antimicrobial peptide with cross-chain interaction between tryptophan and histidine and preparation method thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0015] Design of Antimicrobial Peptides

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

[0017] Arg Trp Phe His Phe Pro Gly Arg Trp Phe His Phe-NH 2

1 5 10 12

[0018] Using the arrangement principle of the β hairpin structure, the interaction of tryptophan and histidine forms the mutual attraction of two β side chains, and the PG corner is used as the central corner unit to design a cross-chain interaction containing tryptophan and histidine Antimicrobial peptide template XWYHYPGXWYHY-NH 2 , wherein X is a positively charged amino acid, Y is a hydrophobic amino acid, when X=R, Y=F, the antimicrobial peptide is named WHFPG. The sequences of the antimicrobial peptides are shown in Table 1.

[0019] Table 1 Amino Acid Sequence of Derived Peptides

[0020]

[0021] The sequence length of WHFPG is 12, two tryptophans and four phenylalanines provide sufficient hydrophobicity, and the corner unit is a PG unit. Containing two arginines and two hist...

Embodiment 2

[0023] Synthesis of WHFPG Antimicrobial Peptide by Solid Phase Chemical Synthesis

[0024] 1. The preparation of antimicrobial peptides is carried out one by one from the C-terminal to the N-terminal, 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 inserted into Wang resin, and then the Fmoc group is removed to obtain X-Wang resin; then Fmoc-Y-Trt-OH (9 -Fmoxy-trimethyl-Y, Y is the second amino acid at the C-terminus 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 side of the Fmoc group is removed chain protection resin;

[0025] 2. Add a cleavage reagent to the peptide resin obtained above, react for 2 hours at 20°C in the dark, filter; wash the precipitate with TFA (trifluoroacetic acid), mix the washing liquid with the above filtrate, concentrate with a rotary evaporator, and t...

Embodiment 3

[0028] Embodiment 3: the mensuration of antimicrobial peptide antibacterial activity

[0029] 1. Determination of antibacterial activity: the determination method adopts the micro broth dilution method. Bacterial strains were incubated overnight at 37 °C with constant shaking at 220 rpm and then transferred to new MHB until log phase of growth. The peptide solution was added to 0.2% bovine serum albumin containing 0.01% acetic acid and serially diluted. 50 μL of bacteria Incubate with 50 μL of bovine serum albumin (pH=7.4 or 6.0) containing different concentrations of peptides at 37° C. for 18-24 hours. Each test was replicated 3 times, and each replicate had 2 parallels. MHB with and without bacteria were used as positive and negative controls, respectively. By measuring the OD at 492 nm, the MIC was calculated as the lowest concentration of the peptide for which no microbial growth was observed both visually and spectrophotometrically. The test results are shown in Tab...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

No PUM Login to View More

Abstract

The invention provides a β-hairpin antimicrobial peptide with cross-chain interaction between tryptophan and histidine and a preparation method thereof. Antimicrobial peptide WHFPG, the sequence of which is shown in SEQ ID No.1. The preparation method utilizes the arrangement principle of the β-hairpin structure to form two β-side chains to attract each other through the interaction of tryptophan and histidine, and uses the PG corner as the central corner unit to obtain a stable β-hairpin two Affinity antimicrobial peptide template XWYHYPGXWYHY‑NH 2 , X=R, Y=F. The application of the antibacterial peptide in the preparation of drugs for treating infectious diseases caused by Gram-positive bacteria and / or Gram-negative bacteria. The antibacterial agent can function under both neutral pH conditions and acidic pH conditions, and can more powerfully inhibit Gram-negative bacteria under acidic pH conditions, with a therapeutic index of 211.68, and has wider clinical application potential.

Description

technical field [0001] The invention belongs to the field of biotechnology, and in particular relates to a β-hairpin antibacterial peptide with cross-chain interaction between tryptophan and histidine and a preparation method thereof. Background technique [0002] The abuse of antibiotics has led to the emergence of a large number of drug-resistant bacteria, especially superbugs, which have developed resistance to multiple antibiotics. Therefore, it is urgent to discover and develop alternative antibacterial materials. Antimicrobial peptides (AMPs) exist in almost all life forms and have a wide range of activities against microbial pathogens. It is generally believed that the main process by which AMP acts on pathogens is to bind cell membranes through electrostatic interactions and form various types of cleavage through physical penetration, resulting in the efflux of the contents. This special mechanism of action makes it difficult for microorganisms to develop resistance...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
Patent Type & Authority Patents(China)
IPC IPC(8): C07K7/08C07K1/06C07K1/04A61K38/10A61P31/04
CPCC07K7/08A61P31/04A61K38/00
Inventor 单安山邵长轩谭鹏
Owner NORTHEAST AGRICULTURAL UNIVERSITY
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic, Popular Technical Reports.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com