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

Recombinant protein for weight loss, vaccine and construction method thereof

A technology of recombinant protein and construction method, applied in the field of vaccines, can solve the problems of drug accumulation, central side effects, accumulation, etc., achieve the effect of increasing secretion, reducing body weight and fat content, and solving long-term use

Active Publication Date: 2019-08-16
HAINAN UNIVERSITY
View PDF4 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0013] From the perspective of drug development, there are certain difficulties in the research of central weight loss drugs
The first difficulty is how to make the drug pass through the blood-brain barrier effectively; the second difficulty is the central side effects caused by the drug
Peripherally acting drugs produce less side effects than centrally acting weight loss drugs, but a potential risk factor for this class of drugs is the possibility of drug accumulation in the liver; another factor worth considering is inhibition of a metabolic enzyme After activity, the substrate of the enzyme has the potential to accumulate in the body

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
  • Recombinant protein for weight loss, vaccine and construction method thereof
  • Recombinant protein for weight loss, vaccine and construction method thereof
  • Recombinant protein for weight loss, vaccine and construction method thereof

Examples

Experimental program
Comparison scheme
Effect test

example

[0100] Example 1-------Construction and expression of recombinant protein 1, including:

[0101] 1) Recombinant protein 1 protein sequence>Protein1LIJUN_20180822:

[0102] MAPQTITELCSEYRNTQIYTINDKILSYTESMAGKREMVIITFKSGETFQVEVPGSQHIDSQKKAIERMKDTLRITYLTETKIDKLCVWNNKTPNSIAAISMKNEFAKFVAAWTLKAAAGSAGCKNFFWKTFTSCLEHHHHHH.

[0103] The first position of the N-terminal is methionine, which is because the expression system of Escherichia coli is used. The 2nd to 104th positions (103AA) of the N-terminus are LTB (Escherichia coli heat-labile enterotoxin B subunit). The 105th-106th position of the N-terminal is the linker sequence EF, the 107-119th position of the N-terminal is the immune enhancement sequence, the 120-121st position of the N-terminal is the linker sequence GS, the 122-135th position is the somatostatin sequence, and the 136th- The 137th position is the linker sequence LE, and the 138-143rd position is the 6His tag.

[0104] Recombinant protein 1 protein gene sequence>P...

example 3

[0120] Example 3-------The immunogenicity of recombinant protein 1, including:

[0121] Immunization: 16 6-week-old Kunming mice (SPF grade, female) were randomly divided into experimental group and control group, with 8 mice in each group, and footpad immunization was carried out on day 0, 21, and 42 respectively. The recombinant protein was used as the immunogen, and the immunization dose was 50 μg per mouse, and the control group was immunized with PBS buffer. One week after the last immunization, blood was collected from the orbital venous plexus of the mice, and the serum was separated and stored at -20°C.

[0122] Tissue section: After blood collection, all mice were killed, dissected, immune-related organs were separated, weighed, fixed with 4% paraformaldehyde, and sent to the company to make pathological sections.

[0123] Western blot: take the purified recombinant protein for SDS-PAGE electrophoresis, cut off the gel containing the target protein after electrophore...

example 4

[0125] Example 4-------Construction and expression of recombinant protein 2, including:

[0126] 1) Recombinant protein 2 protein sequence>Protein2LIJUN_20180822:

[0127] MAPQTITELCSEYRNTQIYTINDKILSYTESMAGKREMVIITFKSGETFQVEVPGSQHIDSQKKAIERMKDTLRITYLTETKIDKLCVWNNKTPNSIAAISMKNEFQYIKANSKFIGITEGSAGCKNFFWKTFTSCLEHHHHHH.

[0128] The first position of the N-terminal is methionine, which is because the expression system of Escherichia coli is used. The 2nd to 104th positions (103AA) of the N-terminus are LTB (Escherichia coli heat-labile enterotoxin B subunit). The 105th-106th position of the N-terminal is the linker sequence EF, the 107-120th position of the N-terminal is the immune enhancement sequence, the 121-122nd position of the N-terminal is the linker sequence GS, the 123-136th position is the somatostatin sequence, and the 137th- The 138th position is the linker sequence LE, and the 139th-144th position is the 6His tag.

[0129] Recombinant protein 2 gene sequence>Protei...

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 belongs to the technical field of vaccines, and discloses a recombinant protein for weight loss, a vaccine and a construction method thereof. The vaccine for weight loss is recombinant protein 1; a protein sequence of the recombinant protein 1 is SEQ ID NO: 1; and a gene DNA sequence of the recombinant protein 1 is SEQ ID NO: 2. The body weight and fat content of nutritional obese mice are effectively reduced by immunizing the recombinant protein with a unique structure and neutralizing somatostatin secreted in the body to relatively increase the secretion amount of growth hormone, so that the problems of long-term use, large adverse reactions, high treatment cost and the like of weight loss drugs in the prior art are solved.

Description

technical field [0001] The invention belongs to the technical field of vaccines, and in particular relates to a recombinant protein for weight loss, a vaccine and a construction method thereof. Background technique [0002] At present, the existing technology commonly used in the industry is as follows: According to the survey, in the past 30 years, the number of overweight and obese people in China has ranked second in the world after the United States, and it has shown "explosive growth in obesity". The World Health Organization recognizes obesity as the largest chronic disease among adults worldwide. [0003] Obesity can be divided into three categories according to the causes of occurrence. The first category is hereditary obesity, which often has a familial obesity tendency. The second category is secondary obesity, which mainly refers to obesity caused by endocrine disorders. The above two types of obese patients account for less than 10% of the entire obese populati...

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): C07K14/245C12N15/21C12N15/70A61K39/108A61P3/04A01K67/027
CPCC07K14/245C12N15/70A61K39/0258A61P3/04A01K67/027A01K2207/10A01K2227/105A01K2267/0362
Inventor 李军贡长慧冯胜沈文静
Owner HAINAN 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