We have located links that may give you full text access.
Structural insights into the binding mode of flavonols with the active site of Matrix MetalloProteinase-9 through molecular docking and Molecular Dynamic Simulations studies.
Journal of Biomolecular Structure & Dynamics 2017 October 26
Cartilage degradation in rheumatoid arthritis is mediated principally by the collagenases and gelatinases. Gelatinase B (also calledMatrix metalloproteinase 9-MMP-9),is a valid target molecule which is known to participate in cartilage degradation as well as angiogenesis associated with the disease and inhibition of its activity shall prevent cartilage damage and angiogenesis. The focus of this study is to investigate the possibilities of MMP-9 inhibition by flavonol class of bioflavonoids by studying their crucial binding interactions at the active site of MMP 9using molecular docking(Glide XP and QPLD) and further improvisation by post docking MM-GBSA and molecular dynamic (MD) simulations. The results show that flavonols can convincingly bind to active site ofMMP-9 asdemonstrated by their stable interactions at the S1' specificity pocket and favourablebinding energies. Gossypin has emerged as a promising candidate with a docking score of -14.618 kcal/mol, binding energy of -79.97 kcal/mol and a stable MD pattern over 15ns. In addition, interaction mechanisms with respect to catalytic site zinc are also discussed.Further, the drug-like charactersofthe ligands were also analysed using ADME analysis.
Full text links
Related Resources
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app
All material on this website is protected by copyright, Copyright © 1994-2024 by WebMD LLC.
This website also contains material copyrighted by 3rd parties.
By using this service, you agree to our terms of use and privacy policy.
Your Privacy Choices
You can now claim free CME credits for this literature searchClaim now
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app