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Title 

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

Authors 

T T H NguyenY H MoonYoung Bae RyuYoung Min KimS H NamM S KimA KimuraD Kim

Publisher 

Elsevier

Issue Date 

2013

Citation 

Enzyme and Microbial Technology, vol. 52, no. 1, pp. 26-31

Keywords 

CatechinEpigallocatechin gallateExpressionInhibitionMatrix metalloproteinase MMP-1Molecular docking

Abstract 

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±1.42μM. The inhibition activity of the nine flavonoid compounds and gallic acid against MMP1ca was examined. Among the compounds tested, the IC50 of seven flavonoid compoundswere determined and ranged from 14.13 to 339.21μM. Epigallocatechin gallate (EGCG) showed the highest inhibition toward MMP1ca with IC50 values of 14.13±0.49μM. EGCG showed a competitive inhibition pattern with a Ki value of 10.47±0.51μM. The free binding energy of EGCG against MMP1ca was -13.07kcalmol-1, which was calculated by using Autodock 3.0.5 software and showed numerous hydrophobic and hydrogen bond interactions. Thegalloyl group of EGCG, gallocatechin gallate and epicatechin gallate was determined to be important for inhibitory activity against MMP1ca.

ISSN 

0141-0229

Link 

http://dx.doi.org/10.1016/j.enzmictec.2012.10.001

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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