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

Use of peptidomimetic compounds in the preparation of drugs for inhibiting intracellular growth of Chlamydia trachomatis

A technology of Chlamydia trachomatis and peptide compounds, which can be applied in the directions of antibacterial drugs, drug combinations, peptides, etc., can solve the problem of not inhibiting Chlamydia trachomatis and the like.

Active Publication Date: 2020-09-01
CENT SOUTH UNIV
View PDF2 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0004] It is reported in the literature that it can be used for the selective transformation of DPPIV / CD26 and can be used for the family of highly lipophilic antiviral drugs [Journal of Medicinal Chemistry (2011), 54 (6), 1927-1942], but there is no information about its inhibition of Chlamydia trachomatis Related reports

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
  • Use of peptidomimetic compounds in the preparation of drugs for inhibiting intracellular growth of Chlamydia trachomatis
  • Use of peptidomimetic compounds in the preparation of drugs for inhibiting intracellular growth of Chlamydia trachomatis
  • Use of peptidomimetic compounds in the preparation of drugs for inhibiting intracellular growth of Chlamydia trachomatis

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0028] The effect of peptidomimetic compound A1 on inhibiting the reproduction of Chlamydia trachomatis. HeLa229 with good logarithmic phase growth was added to each well at 1.5×10 5 A number of cell plates, placed at 37 ° C, 5% CO 2 After routine culture in the cell culture box for 24 hours, wash twice with PBS, add 1 mL of 1640 medium containing 10% fetal bovine serum, and add Chlamydia trachomatis liquid and complete medium at 1:200, 1:400, 1:600, respectively. The protoplasma of Chlamydia trachomatis was added at a ratio of 1:800 and 1:1000, and Hoechst staining was carried out after 24 hours. Randomly select 3 fields of view to count cells and inclusion bodies, and obtain IFU (Inclusion-forming unit, inclusion body forming unit) and MOI (multiplicity of infection, infection copy number, MOI=IFU / cell number), which are used to optimize the optimal detection rate of Chlamydia trachomatis. optimal infectious dose. Furthermore, after infecting HeLa229 cells with L2 serotyp...

Embodiment 2

[0032]The peptidomimetic compound A1 inhibits the normal inclusion body formation of Chlamydia trachomatis.

[0033] image 3 It is an electron micrograph of Chlamydia trachomatis infecting Hela229 cells with compound A1. image 3 It can be seen that the inhibitor of Chlamydia trachomatis HtrA protein causes small inclusion bodies to fail to fuse into large inclusion bodies, and after Chlamydia trachomatis infected Hela229 cells were treated with 10 μM compound A1, there were 4 small inclusion bodies.

[0034] Cytotoxicity test of peptidomimetic compound A1. 5 × 10 3 The number of Hella229 cells was seeded into a 96-well plate, and the cells were placed at 37°C, 5% CO 2 After routine culture in the cell culture box for 24 hours, a control group (Hela229 cells + normal medium), A1 concentration 100 μM + Hela229 cells, and DMSO + Hela229 cell groups were set. Three replicate wells were set up in each group, and the total volume of each well was 100 μL. After 20 h of culture,...

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 application of a mimetic peptide compound in preparing a drug for inhibiting intracellular growth of chlamydia trachomatis. The mimetic peptide compound can directly act on HtrA(High Temperature Requirement A) protein of the chlamydia trachomatis and is capable of inhibiting intracellular growth of the chlamydia trachomatis in the level of 10 muM, the quantity and the areaof chlamydia trachomatis inclusion bodies are reduced, and a new path is provided for treating chlamydia trachomatis infection.

Description

technical field [0001] The invention relates to the technical field of biomedical applications, in particular to the use of a peptidomimetic compound in the preparation of a drug for inhibiting intracellular growth of Chlamydia trachomatis. Background technique [0002] HtrA (High temperature requirement A) is a highly conserved bacterial serine protease, which has molecular chaperone and protease functions, and is a quality control device for proteins. However, unlike other proteases in this family, HtrA from Chlamydia trachomatis is secreted into host cells. Chlamydia trachomatis HtrA can recognize a variety of substrate sequences. After substrate binding, it can induce the conformational change and multimerization of Chlamydia trachomatis HtrA, thereby activating the hydrolysis ability of the enzyme. At present, there is no resolved HtrA protein structure of Chlamydia trachomatis. The HtrA protein of Escherichia coli is called DegP, and its protein crystal structure has...

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): A61K38/07A61P27/02A61P31/02A61P31/04C07K5/083
CPCA61K38/07A61P27/02A61P31/02A61P31/04C07K5/0808
Inventor 王勇王芙艳蔡继峰周亚春陆小芳
Owner CENT SOUTH 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