Anti-tumor-stroma metalloprotease inhibitor

A technology of protease inhibitors and matrix metals, applied in the field of biomedicine, can solve the problems of reducing the selective inhibitory ability of MMPs, and achieve the effects of strong MMPs inhibitory activity, low price, and easy access

Inactive Publication Date: 2009-10-21
NORTHWEST UNIV(CN) +1
View PDF0 Cites 5 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

The zinc ion chelation inhibitor structure itself reduces its selective inhibitory ability to MMPs

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
  • Anti-tumor-stroma metalloprotease inhibitor
  • Anti-tumor-stroma metalloprotease inhibitor
  • Anti-tumor-stroma metalloprotease inhibitor

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0041] Inhibitory effect of aluminum ammonium sulfate on MMP-16: The reaction was carried out in 50mmol / L HEPES buffer system (pH6.8), which contained 200mmol / L NaCl, 10mmol / LCaCl 2 , 20μmol / LZnCl 2 , 10mmol / L MgCl 2 and 0.01% Brij-35. At a certain enzyme concentration, ammonium aluminum sulfate was added to the reaction mixture at different concentrations, placed at 37°C for 30 minutes, and the reaction was initiated by adding 1 μL of 200 μg / ml DQ-gelatin substrate. The inhibition efficiency was determined by comparing the enzyme activity in the presence or absence of the inhibitor. The fluorescence was detected by FLX800 fluorescence microplate reader (Bio-Tek). The excitation wavelength was at 495 nm and the emission wavelength was at 515 nm. All experiments were performed in 96-well plates, and each measurement was corrected for background fluorescence absorption subtracted. It was found that ammonium aluminum sulfate has a good inhibitory effect on MMP-16, and its IC ...

Embodiment 2

[0043] Inhibitory effect of potassium aluminum sulfate on MMP-16: The reaction was carried out in 50mmol / L HEPES buffer system (pH 6.8), which contained 200mmol / L NaCl, 10mmol / LCaCl 2 , 20μmol / LZnCl 2 , 10mmol / L MgCl 2 and 0.01% Brij-35. At a certain concentration of enzyme concentration, potassium aluminum sulfate was added to the reaction mixture at different concentrations, placed at 37°C for 30 minutes, and the reaction was initiated by adding 1 μL of 200 μg / ml DQ-gelatin substrate. The inhibition efficiency was determined by comparing the enzyme activity in the presence or absence of the inhibitor, and the fluorescence was detected by a FLX800 fluorescence microplate reader (Bio-Tek). The excitation wavelength was at 495 nm and the emission wavelength was at 515 nm. All experiments were performed in 96-well plates, and each measurement was corrected for background fluorescence absorption subtracted. It was found that potassium aluminum sulfate has a good inhibitory ef...

Embodiment 3

[0045] Inhibitory effect of aluminum sulfate on MMP-16: The reaction was carried out in 50mmol / L HEPES buffer system (pH6.8), which contained 200mmol / L NaCl, 10mmol / LCaCl 2 , 20μmol / LZnCl 2 , 10mmol / L MgCl 2 and 0.01% Brij-35. At a certain concentration of enzyme concentration, aluminum sulfate was added to the reaction mixture at different concentrations and placed at 37°C for 30 minutes. The reaction was initiated by adding 1 μL of 200 μg / ml DQ-gelatin substrate. The inhibition efficiency was determined by comparing the enzyme activity in the presence or absence of the inhibitor. The fluorescence was detected by a FLX800 fluorescence microplate reader (Bio-Tek), and the excitation wavelength was 495 nm. , the emission wavelength is 515nm. All experiments were performed in 96-well plates, and each measurement was corrected for background fluorescence absorption subtracted. It was found that aluminum sulfate has a good inhibitory effect on MMP-16, and its IC 50 is 1.56 μm...

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 a use of third-valence metal salt as MMPs inhibitor, the third-valence metal salt is free third-valence metal salt or third-valence metal composition. The third-valence metal salt is third-valence rare earth salt or third-valence transition metal salt or third-valence major-group metal salt. Compared with prior MMPs inhibitor, the third-valence metal salt of the invention has relatively strong MMPs inhibiting activity; furthermore, the third-valence metal salt of the invention has simple structure, low cost and convenient availability.

Description

[0001] Field of study [0002] The invention belongs to the technical field of biomedicine, and particularly relates to a class of anti-tumor matrix metalloproteinase inhibitors. Background technique [0003] In recent years, research in the field of anti-tumor matrix metalloproteinases (MMPs) has progressed rapidly, and all 23 human-derived MMPs have been cloned. In the process of tumor cell invasion and metastasis, cancer cells first need to degrade extracellular matrix (ECM) and basement membrane (BM). The degradation of ECM components is a necessary step for cancer cell invasion and metastasis. And this degradation function is mainly completed by proteolytic enzymes. MMPs are an important class of proteolytic enzymes, and they are one of the most important ECM-degrading proteases. MMPs can enhance tumor angiogenesis and promote cancer cell invasion and metastasis by degrading the basement membrane and vascular matrix. Since MMPs play an important role in tumor invasion 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): A61K33/06A61K33/24A61K33/26A61K33/42A61P35/00
Inventor 申烨华李聪田渭花房学迅蒋坤
Owner NORTHWEST UNIV(CN)
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
Try Eureka
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap