Design, synthesis and activity evaluation of novel matrix metalloproteinases inhibitors based on the structure of enzyme.
- Author:
Hong JIA
1
;
Yan-shen GUO
;
Yi-yu GE
;
Hui WEN
;
Jing YANG
;
Xiu-ying YANG
;
Guan-hua DU
;
Guang-zhong YANG
Author Information
1. Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union'Medical College, Beijing 100050, China.
- Publication Type:Journal Article
- MeSH:
Drug Design;
Enzyme Inhibitors;
chemical synthesis;
chemistry;
Matrix Metalloproteinase Inhibitors;
Matrix Metalloproteinases;
chemical synthesis;
chemistry;
Molecular Structure;
Structure-Activity Relationship
- From:
Acta Pharmaceutica Sinica
2007;42(12):1271-1281
- CountryChina
- Language:Chinese
-
Abstract:
A novel inhibitor series for matrix metalloproteinases (MMPs) were designed and synthesized. Using succinate and malonate as zinc binding groups and long hydrophobic substituents to bind with S1' pockets, the compounds showed micromolar inhibition and selectivity for MMP-2 over others. And we found a better activity compound. It is a chance to find a better precursor of MMP-2 inhibitors with activity and bioavailability by further optimization of compounds.
