Eureka AIR delivers breakthrough ideas for toughest innovation challenges, trusted by R&D personnel around the world.

Gene of encoded antibacterial peptide, gene of fusion protein and recombinant vector

A fusion protein and antimicrobial peptide technology, which is applied in the direction of virus/phage, recombinant DNA technology, and the use of vectors to introduce foreign genetic material, etc., can solve problems such as high treatment costs, poor treatment compliance, and bacterial drug resistance

Inactive Publication Date: 2018-01-09
ANHUI SCI & TECH UNIV
View PDF1 Cites 4 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, with the increase of antibiotic-resistant strains, re-infection, complications, high treatment costs and poor treatment compliance, the eradication of antibiotics to Helicobacter pylori infection is limited, and the main reason is bacterial resistance

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
  • Gene of encoded antibacterial peptide, gene of fusion protein and recombinant vector
  • Gene of encoded antibacterial peptide, gene of fusion protein and recombinant vector
  • Gene of encoded antibacterial peptide, gene of fusion protein and recombinant vector

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0123] This embodiment provides an antibacterial peptide with anti-H. pylori activity, the amino acid sequence of which is shown in SEQ ID NO:1.

[0124] The screening and experimental process of this antimicrobial peptide are as follows:

[0125] a. Screening of antimicrobial peptides: Antimicrobial peptides have their own unique antibacterial spectrum just like antibiotics. Not all antimicrobial peptides have antibacterial activity against Helicobacter pylori. There are 25 kinds of antibacterial peptides against Gram-negative bacteria, which are synthesized by chemical methods.

[0126] b. Antimicrobial peptide preparation: According to the minimum inhibitory concentration test method, the chemically synthesized antimicrobial peptides were diluted to 64μg / mL, 32μg / mL, 16μg / mL, 8μg / mL, 4μg / mL, 2μg / mL, 1μg / mL, 0.5μg / mL.

[0127] c. Detect the minimum inhibitory concentration: add the logarithmic Helicobacter pylori ATCC34504 standard bacterial strain in each test tube to re...

Embodiment 2

[0130] The present embodiment simulates the gastric environment to carry out antibacterial effect test to the antimicrobial peptide PGQ that embodiment 1 provides:

[0131] a. Preparation of artificial gastric juice (containing pepsin and gastric acidic substances, pH 1.3-1.8);

[0132] b. Culture different strains of Helicobacter pylori, including: ATCC34504 standard strain and clinical strains isolated from gastric ulcer and gastric cancer patients.

[0133] c. Add log phase Helicobacter pylori 10 to artificial gastric juice 6 CFU / mL, then add antimicrobial peptide PGQ to achieve a concentration of 4 μg / mL (4×MIC) and no antimicrobial peptide as the control group, take 10 μL of the mixed solution at 15 min, 30 min, 60 min and 120 min to dilute to 50 μL, and apply In solid medium, count the colonies on each plate after culturing for 36 h. Calculate the sterilization rate according to the formula:

[0134] Bactericidal rate=(1-the number of colonies on the bacteria liquid p...

Embodiment 3

[0137] The antibacterial peptide PGQ provided by Example 1 with anti-H. If it is directly expressed in a large amount in the host cell, it will have a great impact on the physiological pH of the host cell, and then affect the survival of the host cell, which is not conducive to the high-level expression of the antimicrobial peptide PGQ. In fact, the inventors found in experiments that if the antimicrobial peptide is directly expressed without fusion, the antimicrobial peptide cannot be expressed in the host cell at all.

[0138] In view of this, this embodiment provides a fusion protein for expressing the antimicrobial peptide PGQ, the fusion protein has the following primary amino acid sequence structure:

[0139] Carrier protein-connecting peptide-protease action site peptide-antibacterial peptide;

[0140] Wherein, the carrier protein includes Bombyx mori baculovirus nuclear polyhedrin, glutathione sulfhydryl transferase, green fluorescent protein, or ubiquitin-like small ...

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 gene of an encoded antibacterial peptide, a gene of fusion protein and a recombinant vector and belongs to the field of pharmaceutics. The amino acid sequence of the antibacterial peptide is shown as SEQ ID NO: 1. The fusion protein has the following primary amino acid sequence structure: vector protein-connecting peptide-antibacterial peptide, wherein the antibacterial peptide has the amino acid sequence shown as SEQ ID NO: 1. The antibacterial peptide provided by the invention has helicobacter pylori resisting activity and has relatively strong stability and antibacterial activity in a stomach environment; a cell membrane is perforated through a physical effect and the effect of resisting helicobacter pylori is realized; the helicobacter pylori does not easily have drug resistance in a utilization process of the antibacterial peptide.

Description

technical field [0001] The invention relates to the field of pharmacy, in particular to a gene encoding an antimicrobial peptide, a gene for a fusion protein and a recombinant vector. Background technique [0002] Helicobacter pylori was discovered by two Australian scientists in the 1980s and won the Nobel Prize in Physiology in 2005. At present, more than 50% of the world's population is infected with this pathogen, and 20% of those infected will cause clinical symptoms of chronic gastritis, peptic and duodenal ulcers, gastric cancer, and mucosa-associated lymphoid tissue tumors. The World Health Organization has listed it as a class I carcinogen. It is more popular in developing countries, and the infection rate of the population in some areas of our country is as high as 60%. [0003] Antibiotics are an effective way to treat Helicobacter pylori infection, but Helicobacter pylori is resistant to multiple antibiotics, and even the same infected patient is resistant to 7...

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): C07K14/00C12N15/62C12N15/63C12N1/21C12N5/10C12N7/01
Inventor 张孝林汪建飞蒋安民贡成良范涛张钦元
Owner ANHUI SCI & TECH UNIV
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
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