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

Para-cecropin antibacterial peptide and application thereof

A cecropin antimicrobial peptide and antimicrobial peptide technology, applied in the field of molecular biology, can solve the problems of unsatisfactory antibacterial activity, cytotoxicity, and low yield of antimicrobial peptide, and achieve good application prospects, strong antibacterial activity, and antibacterial effect Good results

Active Publication Date: 2014-11-12
HENAN UNIV OF SCI & TECH
View PDF2 Cites 5 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, compared with traditional antibiotics, the yield of antimicrobial peptides from natural sources is low, the antibacterial activity is not ideal, and some even have cytotoxicity.

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
  • Para-cecropin antibacterial peptide and application thereof
  • Para-cecropin antibacterial peptide and application thereof
  • Para-cecropin antibacterial peptide and application thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0021] The cecropin-like antimicrobial peptide in this example has an amino acid sequence of: SWLSKTAKKLFKKIPKKRFPRPRPWPRPNMI (same as shown in SEQ ID NO.1), and a molecular weight of 3833.7Da. The antimicrobial peptide contains cecropin S-W-L-S-K-T-A-K-K-L-F antibacterial active structure, rich in arginine (Arg) and lysine (Lys), and arginine (Arg) and lysine (Lys) residues are positively charged to attract bacterial surface negative charge. At the same time, the basic structural unit R-P-R-P-W-P-R-P forms a double-sided hydrophobic α-helix structure.

[0022] The cecropin-like antimicrobial peptide in this example was synthesized by Shanghai Tricapeptide Biotechnology Co., Ltd. by solid-phase synthesis, with a purity greater than 95%.

Embodiment 2

[0024] In this example, the application of cecropin-like antibacterial peptides in the preparation of antibacterial drugs, the amino acid sequence of the antibacterial peptides is: SWLSKTAKKLFKKIPKKRFPRPRPWP RPNMI, and the molecular weight is 3833.7Da. The cecropin-like antimicrobial peptide is made into a cecropin-like polypeptide tablet by a conventional method, and the main drug cecropin-like antibacterial peptide has a content of 0.2 g per tablet, and the mass percentage of the main drug is 50%, and the auxiliary materials are starch, sucrose , Composed of talcum powder.

Embodiment 3

[0026] In this example, the application of cecropin-like antibacterial peptides in the preparation of antibacterial drugs, the amino acid sequence of the antibacterial peptides is: SWLSKTAKKLFKKIPKKRFPRPRPWP RPNMI, and the molecular weight is 3833.7Da. The cecropin-like antimicrobial peptide is made into cecropin-like peptide sodium chloride injection by conventional method, and every 100mL injection is made up of the following components: main drug cecropin-like antimicrobial peptide 0.2g, sodium chloride 0.9g, and the remaining The amount is water for injection.

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

PropertyMeasurementUnit
Diameteraaaaaaaaaa
Molecular weightaaaaaaaaaa
Login to View More

Abstract

The invention discloses a para-cecropin antibacterial peptide and application thereof and belongs to the technical field of molecular biology. The para-cecropin antibacterial peptide consists of 31 amino acids and has the molecular weight of 3833.7Da. The antibacterial peptide can be used for inhibiting the growth of bacteria, such as staphylococcus aureus, avian pasteurella multocida, salmonella gallinarum and avian escherichia coli, has a better bacteriostasis effect compared with the commonly-used antibiotics, such as penicillin, streptomycin, cefazolin sodium and azithromycin, and has stronger bacteriostasis activity compared with the conventional cecropin antibacterial peptides, such as Cecropin B, Cecropin A and Cecropin P1. The antibacterial peptide has the minimum salmonella gallinarum bacteriostasis concentration of 625 micrograms per milliliter, has good thermal stability and has good application prospect in the research and development of antibacterial drugs.

Description

technical field [0001] The invention relates to a cecropin-like antibacterial peptide and the application of the antibacterial peptide, belonging to the technical field of molecular biology. Background technique [0002] Antibacterial peptides (Antibacterial peptides) are a class of small molecular polypeptides that are encoded by specific genes in various biological cells and induced by external conditions. The world's first antimicrobial peptide was discovered by Swedish scientist G.Boman et al. in 1980 from silkworm chrysalis. Since then, people have successively discovered and isolated a variety of antimicrobial peptides in various organisms such as bacteria, fungi, plants, insects, amphibians, birds, fish, mammals and even humans. So far, more than 2,000 kinds of antimicrobial peptides have been identified and isolated from reports at home and abroad, and thousands of mimetic peptides have been artificially synthesized using natural antibacterial peptides as templates....

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
IPC IPC(8): C07K14/00A61K38/16A61P31/04
CPCA61K38/00C07K14/4723Y02A50/30
Inventor 王臣汪洋郭香玲牛明媚吴庭才
Owner HENAN UNIV OF SCI & TECH
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