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

Defensin cathelicidin-PP of polypedates puerensis as well as gene and application thereof

A defense peptide, tree frog technology, applied in the field of biomedicine, to inhibit the growth of bacteria and fungi

Active Publication Date: 2017-05-31
KUNMING MEDICAL UNIVERSITY
View PDF1 Cites 9 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Puer tree frog Polypedates puerensis is mainly distributed in the surrounding areas of Puer City, Yunnan Province. It is one of the characteristic resource animals in my country. The antibacterial peptides of the cathelicidin family in its skin secretions have not been reported yet.

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
  • Defensin cathelicidin-PP of polypedates puerensis as well as gene and application thereof
  • Defensin cathelicidin-PP of polypedates puerensis as well as gene and application thereof
  • Defensin cathelicidin-PP of polypedates puerensis as well as gene and application thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment Construction

[0020] The present invention will be described in detail below in conjunction with the accompanying drawings.

[0021] 1. Preparation and amino acid sequence determination of tree frog defense peptide cathelicidin-PP:

[0022] 1. Collect tree frog skin secretions:

[0023] Live tree frogs were cleaned with water and placed in a cylindrical sample bottle with a diameter of 10 cm and a height of 10 cm. After ether stimulation for 2 minutes, the frog's back foam was rinsed with 10 ml of 0.1M pH 6.0 phosphate buffered saline (PBS). The secreted liquid was centrifuged at 12000 rpm for 15 minutes at 4°C, and the supernatant was stored at -80°C. 2. Separation and purification of tree frog defense peptide cathelicidin-PP:

[0024] Using the supernatant collected above as a raw material, the defense peptide cathelicidin-PP was purified according to the following procedures, and each component of the separation and purification was tested for antibacterial activity. The specific meth...

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
molecular weightaaaaaaaaaa
Login to View More

Abstract

The invention relates to defensin cathelicidin-PP of polypedates puerensis as well as a gene and application thereof, and belongs to the field of biomedicine. The defensin cathelicidin-PP is a cyclic polypeptide encoded by a gene of defensin of Chinese amphibian polypedates puerensis, and has a molecular weight of 3,366.08 daltons and an isoelectric point of 10.05; the amino acid sequence of the defensin cathelicidin-PP is as shown by SEQ ID NO: 1. A gene GenBank Accession KY610282 for encoding a precursor of the defensin cathelicidin-PP of the polypedates puerensis consists of 615 nucleotide sequences; the nucleotide sequence of the gene GenBank Accession KY610282 is as shown by SEQ ID NO: 2, wherein nucleotides at No. 346 to No. 441 sites are encoding genes of defensin cathelicidin-PP of mature polypedates puerensis. The invention relates to the application of the defensin cathelicidin-PP of the polypedates puerensis to the preparation of a therapeutic medicine for infectious diseases caused by escherichia coli, salmonella paratyphi A, pseudomonas aeruginosa and candida glabrata. The defensin cathelicidin-PP has the obvious effects of inhibiting the growth of a bacterium and a fungus for the escherichia coli, the salmonella paratyphi A, the pseudomonas aeruginosa and the candida glabrata.

Description

[0001] Technical field: [0002] The invention relates to a tree frog (Polypedates puerensis) defense peptide cathelidin-PP and its gene and application, belonging to the field of biomedicine. [0003] Background technique: [0004] Research in recent years has shown that antimicrobial peptides are an important part of the defense system of all animals, plants and microorganisms. They are a type of small molecular active polypeptides produced by the body to resist the invasion of pathogenic microorganisms. They have the characteristics of small molecular weight, good stability, rapid sterilization and resistance to drug resistance. These characteristics make antimicrobial peptides have very broad application prospects, and are expected to replace traditional antibiotics that are prone to drug resistance in clinical practice. The reason why antimicrobial peptides are not easy to produce drug resistance is that their bactericidal mechanism is different from that of traditional a...

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 Applications(China)
IPC IPC(8): C07K14/46C12N15/12A61K38/17A61P31/04A61P31/10
CPCA61K38/00C07K14/463Y02A50/30
Inventor 杨海龙武静木丽仙刘彤
Owner KUNMING MEDICAL 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