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

Oligopeptide as well as derivatives and application thereof

A technology of derivatives and oligopeptides, applied in the field of oligopeptides and their derivatives and applications, can solve the problems of difficult synthesis and large molecular weight, and achieve the effects of small molecular weight, easy synthesis, and inhibition of influenza virus activity

Active Publication Date: 2018-09-04
CHINA PHARM UNIV
View PDF4 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0006] Aiming at the problem that the existing anti-influenza virus peptides have relatively large molecular weight and are difficult to synthesize, the present invention provides an oligopeptide and its derivatives and applications. The number of amino acids of this type of polypeptide is less than 7, the molecular weight is small, easy to synthesize and has Inhibits the activity of influenza virus and can specifically bind to the hemagglutinin site, suggesting that it has important development and application value in anti-influenza virus therapy

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
  • Oligopeptide as well as derivatives and application thereof
  • Oligopeptide as well as derivatives and application thereof
  • Oligopeptide as well as derivatives and application thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0035] Virus virulence assay (TCID 50 )

[0036] Influenza H1N1 (FM1), H3N2 (N3), H5N1 and H7N9 virus antigens used in the present invention are virus inactivated antigens with hemagglutination activity, all can cause disease, H1N1, H3N2 are human influenza, H5N1 and H7N9 It is bird flu. Taking H7N9 as an example, the virus virulence was tested to prove its activity. The specific experimental steps and results are as follows:

[0037] After the MDCK cells (influenza virus susceptible canine kidney passage cell strain) in the logarithmic growth phase are laid on a single layer, the influenza virus H1N1 is continuously diluted by 10 times, and 10 -2 ~10 -10 The diluted virus was inoculated into MDCK cells, adsorbed at 37°C for 1 hour, washed twice with PBS, and then replaced with maintenance medium to continue culturing. Normal cells were used as controls, and each well had 4 replicate wells. Observe the cell lesion under an inverted microscope every day, record the lesion de...

Embodiment 2

[0046] The present invention uses the protein database (Protein Data Bank) hemagglutinin protein (4BSE) crystal structure as the basis of research, screens out a series of oligopeptides with antiviral activity, its sequence contains X-Y-Leu-Arg-Ala domain, A class of oligopeptide derivatives is obtained by modifying the short peptide X-Y-Leu-Arg-Ala with stearic acid. The general structural formula of this kind of oligopeptide derivatives is C 17 h 35CO-X-Y-Leu-Arg-Ala, wherein X is a positively charged amino acid (such as Lys, His, Arg, etc.); Y is a hydrophobic or positively charged amino acid (such as Pro, Lys, Leu, etc.). These oligopeptide derivatives all have antiviral activity and are expected to be developed into ideal antiviral drugs. The specific structure of oligopeptide derivatives can be:

[0047] Oligopeptide I, C 17 h 35 CO-Lys-Pro-Leu-Arg-Ala; or

[0048] Oligopeptide II, C 17 h 35 CO-His-Pro-Leu-Arg-Ala; or

[0049] Oligopeptide III, C 17 h 35 CO-Ar...

Embodiment 3

[0057] Anti-influenza virus efficacy test method:

[0058] Take cells in good logarithmic growth phase, add 0.25% trypsin digestion solution, blow evenly after digestion and fall off, count, and press 2×10 5 cells / well, seeded in 96-well cell culture plate, placed in constant temperature CO 2 Cultivate in the incubator for 16-24h. Set up normal cell control group, virus infection group, positive drug control group and test drug group respectively. Discard the culture medium, wash three times with PBS, add 100TCID to each well except the normal control group 50 Infectious amount of influenza virus, placed in constant temperature CO 2 The incubator was left to rest for 1 hour, unadsorbed virus was discarded, washed twice with PBS, and then drug-containing maintenance solutions with different concentrations were added. There were 6 doses in the test drug group, each with 3 replicate wells. Then continue to cultivate the cell culture plate with the above-mentioned scheme at 3...

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 discloses oligopeptide as well as derivatives and application thereof, and belongs to the technical field of biological medicine. The sequence of the oligopeptide comprises a structuraldomain X-Y-Leu-Arg-Ala, and the structural general formula of the derivatives of the oligopeptide is C17H35CO-X-Y-Leu-Arg-Ala, wherein X is amino acid with positive charges (such as Lys, His and Arg);and Y is amino acid with hydrophobicity or with positive charges (such as Pro, Lys and Leu). The number of the polypeptide amino acid screened by the invention is less than 7. An experimental resultshows that the polypeptide can obviously inhibit proliferation of anti-influenza viruses, thereby prompting that the polypeptide has important development and application values in anti-influenza virus treatment, and can be applied to preparation of anti-influenza medicines.

Description

technical field [0001] The invention belongs to the technical field of biomedicine, and more specifically relates to an oligopeptide and its derivatives and applications. Background technique [0002] Influenza, as an acute respiratory infectious disease that seriously endangers human health, causes about 500 million people to become sick each year, of which 250,000 to 500,000 people die, and the annual incidence rate in my country is about 10% to 30%. What is even more worrying is that in recent years, the number of human infections with highly pathogenic and fatal influenza virus H5N1 and H1N1 subtypes has been increasing, and the mortality rate is quite high. One of the main reasons for the raging influenza virus is its strong ability to mutate antigens, which makes the immune protection of the vaccine limited. Moreover, the vaccine can only prevent known influenza virus subtypes, and it is not effective against those caused by antigenic drift or conversion. The resultin...

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): C07K7/06A61K38/08A61K47/54A61P31/16
CPCA61K38/00A61K47/542A61P31/16C07K7/06C07K19/00
Inventor 牛淼淼徐寒梅
Owner CHINA PHARM UNIV
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