Role of green tea polyphenols in the inhibition of collagenolytic activity by collagenase

Inhibitory effect of green tea polyphenols viz., catechin and epigallocatechin gallate (EGCG) on the action of collagenase against collagen has been probed in this study. Catechin and EGCG treated collagen exhibited 56 and 95% resistance, respectively, against collagenolytic hydrolysis by collagenas...

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Bibliographic Details
Published in:International journal of biological macromolecules 2007-06, Vol.41 (1), p.16-22
Main Authors: Madhan, B., Krishnamoorthy, G., Rao, J. Raghava, Nair, Balachandran Unni
Format: Article
Language:English
Subjects:
Animals
Catechin - analogs & derivatives
Catechin - chemistry
Catechin - pharmacology
Circular Dichroism
Collagen
Collagen - metabolism
Collagenase
Enzyme Inhibitors - chemistry
Enzyme Inhibitors - pharmacology
Flavonoids - chemistry
Flavonoids - pharmacology
In Vitro Techniques
Kinetics
Male
Matrix Metalloproteinase Inhibitors
Models, Molecular
N-(3-[2-Furyl]acryloyl)-Leu-Gly-Pro-Ala (FALGPA)
Phenols - chemistry
Phenols - pharmacology
Polyphenols
Protein Conformation - drug effects
Rats
Rats, Wistar
Tea - chemistry
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Summary:Inhibitory effect of green tea polyphenols viz., catechin and epigallocatechin gallate (EGCG) on the action of collagenase against collagen has been probed in this study. Catechin and EGCG treated collagen exhibited 56 and 95% resistance, respectively, against collagenolytic hydrolysis by collagenase. Whereas direct interaction of catechin and EGCG with collagenase exhibited 70 and 88% inhibition, respectively, to collagenolytic activity of collagenase against collagen and the inhibition was found to be concentration dependent. The kinetics of inhibition of collagenase by catechin and EGCG has been deduced from the extent of hydrolysis of (2-furanacryloyl- l-leucyl-glycyl- l-prolyl- l-alanine), FALGPA. Both catechin and EGCG exhibited competitive mode of inhibition against collagenase. The change in the secondary structure of collagenase on treatment with catechin and EGCG has been monitored using circular dichroism spectropolarimeter. CD spectral studies showed significant changes in the secondary structure of collagenase on treatment with higher concentration of catechin and EGCG. Higher inhibition of EGCG compared to catechin has been attributed to the ability of EGCG to exhibit better hydrogen bonding and hydrophobic interaction with collagenase.
ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2006.11.013