Journal
ENZYME AND MICROBIAL TECHNOLOGY
Volume 52, Issue 1, Pages 26-31Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.enzmictec.2012.10.001
Keywords
Matrix metalloproteinase MMP-1; Expression; Inhibition; Catechin; Epigallocatechin gallate; Molecular docking
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Funding
- National Research Foundation of Korea (NRF)
- Korea government (MEST) [2012-0007288, 2012R1A2A2A01045995]
- Chonnam National University
- FKPPL Internal Associated Laboratory
- National Research Foundation of Korea [2012R1A2A2A01045995] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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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 K-m value of 26.61 +/- 1.42 mu 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 mu M. Epigallocatechin gallate (EGCG) showed the highest inhibition toward MMP1ca with IC50 values of 14.13 +/- 0.49 mu M. EGCG showed a competitive inhibition pattern with a K-i value of 10.47 +/- 0.51 mu M. The free binding energy of EGCG against MMP1ca was -13.07 kcal mol(-1), which was calculated by using Autodock 3.0.5 software and showed numerous hydrophobic and hydrogen bond interactions. The galloyl group of EGCG, gallocatechin gallate and epicatechin gallate was determined to be important for inhibitory activity against MMP1ca. (C) 2012 Elsevier Inc. All rights reserved.
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