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

Low hemolytic antibacterial peptide and its application

A peptide, antibacterial activity technology, applied in the field of antibacterial peptides, can solve problems such as limiting the development of treatment, achieve the effect of inhibiting growth, improving compatibility, treating or preventing bacterial or viral infection

Inactive Publication Date: 2008-05-28
PACGEN BIOPHARMLS
View PDF7 Cites 1 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, while all have broad antimicrobial potency, these peptides have different hemolytic activities on red blood cells, a property that greatly limits therapeutic development

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
  • Low hemolytic antibacterial peptide and its application
  • Low hemolytic antibacterial peptide and its application
  • Low hemolytic antibacterial peptide and its application

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0083] Example 1: Design, synthesis, purification and characteristics of peptides

[0084] The peptide analogs of the present invention and their nomenclature are shown in Table 1 below, and each amino acid is represented by three letters.

[0085] Table I

[0086]

[0087] C: Cyclic: L: Linear

[0088] All linear peptides were synthesized by solid-state synthesis using standard Fmoc: (N-(9-fluorenyl)methoxycarbonyl) in PAL resin (5-(4-Fmoc-aminomethyl-3, 5-dimethoxyphenoxy)-pentanoic acid-methylphenylhydramine resin) by chemical synthesis; and the Fmoc protecting group on these resins was synthesized with 20% hexahydropyridine / dimethylformamide (piperidine / DMF) Removal, the reaction time is about 1 to 1.5 hours, and then determined by water and ninhydrin test (ninhydrin test). Next, 95% trifluoroacetic acid (TFA) was added and mixed for 1-1.5 hours, and the unprocessed peptide was excised from the resin; then analyzed and purified by reverse-phase high-performance liqui...

Embodiment 2

[0089] Example 2: In vitro peptide activity test

[0090] In general, in vitro peptide antibacterial activity can be tested using the standard National Council for Clinical Laboratory Standards (NCCLS) bacterial inhibition assay or minimum inhibitory concentration (MIC). The so-called minimum inhibitory concentration refers to the minimum peptide concentration required to inhibit or reduce the growth of microorganisms. The organisms tested by the minimum inhibitory concentration analysis method are shown in Table 2:

[0091] Table II

[0092]

[0093]

[0094] Simply put, the overnight cultured bacterial solution was diluted with Meuller-Hinton growth medium to contain approximately 10 5 The inoculum of each colony; the peptide was also serially diluted twice, and then added to the diluted bacterial solution. After culturing at 37°C for 18 hours, analyze its turbidity; the minimum inhibitory concentration of each peptide was measured three times at different times, an...

Embodiment 3

[0100] Example 3: Analysis of Membrane Penetration

[0101] Peptide outer membrane penetration was determined by the 1-N-phenylnaphthylamine (NPN) uptake test. Intact Escherichia coli cell NPN shows weak fluorescence absorption in a liquid environment; while it has a strong absorption value in a water-repellent environment, thus indicating that the NPN is water-repellent and can be used to directly measure the degree of outer membrane penetration. Under normal circumstances, Escherichia coli absorbs little or no NPN; in the presence of some membrane-penetrating compounds (ethylenediaminetetraacetic acid, polymyxin B, neomycin or Antimicrobial peptides), NPN will partially penetrate the outer membrane of bacteria and cause an increase in fluorescence absorption.

[0102] The experimental steps are briefly described as follows: Add 1 ml of overnight cultured bacteria solution to 50 ml of culture solution, shake and culture at 37 degrees to OD 600 Equal to 0.4-0.6, centrifuge t...

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

An antibacterial with cyclic short chain and low hematolysis has the chemical formula (A1X1A2)N and unique amino acid structure with benzene ring and positive charge.

Description

technical field [0001] The invention relates to an antibacterial peptide, especially a short peptide with a ring structure and only composed of 9 benzene rings and positively charged amino acids. The peptide has excellent antibacterial ability. Compared with other long peptides also composed of benzene rings and positively charged amino acids, this short peptide exhibits excellent antibacterial efficacy and low hemolytic activity. Background technique [0002] The emergence of strains resistant to traditional antibiotics has spurred the search for novel therapeutic agents, including many antimicrobial peptides of animal origin. It is now found that these antimicrobial peptides play a very important role in the innate defense mechanism of some hosts, including plants, insects, amphibians and mammals. These peptides may also have antibiotic activity against bacteria, fungi, and even some viruses, which can bind lipids (greater than 95 percent), rapidly dissociate the lipid bi...

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): C07K7/06C07K7/64A61K38/10A61K38/12A61P31/04A61P31/12
Inventor 曾秀如程家维
Owner PACGEN BIOPHARMLS
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