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The influence of flavonoid compounds on the in vitro inhibition study of a human fibroblast collagenase catalytic domain expressed in E coli

Enzyme and Microbial Technology. 2013-01; 
Thi Thanh HanhNguyenaYoung-HwanMoonbYoung-BaeRyucYoung-MinKimcSeung-HeeNamdMi-SookKimeAtsuoKimurafDomanKim
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Custom Vector Construction … The catalytic domain of the MMP1 cDNA encoding human fibroblast collagenase (GenBank accession no. X05231) was constructed (GenScript, Piscataway, NJ, USA) and cloned into the pUC57 vector (pUC57-MMP1ca). The … Get A Quote

摘要

The human fibroblast collagenase catalytic domain (MMP1ca) that is considered a prototype for all interstitial collagenase and plays an important role in the turnover of collagen fibrils in the matrix was expressed as an inclusion body in the Escherichia coli. The purified enzyme displayed activity with substrate Dnp-Pro-Leu-Ala-Leu-Trp-Ala-Arg-OH with a Km value of 26.61 ? 1.42 ?M. The inhibition activity of the nine flavonoid compounds and gallic acid against MMP1ca was examined. Among the compounds tested, the IC50 of seven flavonoid compounds were determined and ranged from 14.13 to 339.21 ?M. Epigallocatechin gallate (EGCG) showed the highest inhibition toward MMP1ca with IC50 values of 14.13 ? 0.49 ?M. EG... More

关键词

Matrix metalloproteinase MMP-1ExpressionInhibitionCatechinEpigallocatechin gallateMolecular docking