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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

Paper ID Volume ID Publish Year Pages File Format Full-Text
17152 42647 2013 6 PDF Available
Title
The influence of flavonoid compounds on the in vitro inhibition study of a human fibroblast collagenase catalytic domain expressed in E. coli
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 ± 1.42 μM. 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 μM. Epigallocatechin gallate (EGCG) showed the highest inhibition toward MMP1ca with IC50 values of 14.13 ± 0.49 μM. EGCG showed a competitive inhibition pattern with a Ki value of 10.47 ± 0.51 μM. 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.

Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► The expression and biochemical characterization of catalytic domain of MMP1. ► Examined the inhibition of nine flavonoid compounds and gallic acid against MMP1ca. ► Structure–activity relationship between the flavonoids and MMP1ca. ► Competitive inhibition study of EGCG against MMP1ca. ► Analysis of the binding mode of EGCG in active site pocket of MMP1ca.

Keywords
MMPs, matrix metalloproteinases; MMP8, neutrophil collagenase; MMP13, collagenase 3; EGCG, epigallocatechin gallate; MMP1ca, catalytic domain of MMP1; SAR, the structure–activity relationship; SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electropho
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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
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 52, Issue 1, 10 January 2013, Pages 26–31
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us