2007
DOI: 10.1016/j.ijbiomac.2006.11.013
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Role of green tea polyphenols in the inhibition of collagenolytic activity by collagenase

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Cited by 145 publications
(114 citation statements)
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“…There are many hydroxyl groups present in the TA which can act as hydrogen bond donor/ acceptor with different side chain groups of amino acids of collagen namely, aspartic acid (Asp), asparagine (Asn), hydroxyproline (Hyp), lysine (Lys) and serine (Ser). Previous report has also indicated the interaction of collagen with green tea polyphenol 27 . In addition, vegetable tannins have a long history of use in stabilizing collagen in the leather industry and are known to strongly binding to collagens 28 .…”
Section: Collagen-ta Interactionsmentioning
confidence: 86%
See 1 more Smart Citation
“…There are many hydroxyl groups present in the TA which can act as hydrogen bond donor/ acceptor with different side chain groups of amino acids of collagen namely, aspartic acid (Asp), asparagine (Asn), hydroxyproline (Hyp), lysine (Lys) and serine (Ser). Previous report has also indicated the interaction of collagen with green tea polyphenol 27 . In addition, vegetable tannins have a long history of use in stabilizing collagen in the leather industry and are known to strongly binding to collagens 28 .…”
Section: Collagen-ta Interactionsmentioning
confidence: 86%
“…We found that TA is a competitive mode of inhibition of ChC activity, with a K i of 20 µM against FALGPA degradation. Previously, we reported the kinetics of inhibition of ChC by green tea polyphenolics 27 . Based on the accepted hydrolysis scheme for FALGPA by ChC 16 , TA can interact with ChC at site of the free ChC to form ChC-TA complex.…”
Section: Chc Inhibition Kineticsmentioning
confidence: 99%
“…Hydroxyl groups of polyphenol could interact with the backbone or other functional group side chain of collagenase. In addition, hydrophobic interaction between the benzene ring of polyphenol and collagenase could also result in the conformational changes leading to unfunctioned enzyme (Madhan et al 2007). Another mechanism involves the Zn ion active site on collagenase.…”
Section: Discussionmentioning
confidence: 99%
“…By hydrogen bonding and hydrophobic interactions with the collagenase, EGCG might lead to conformational changes or to masking of the catalytic region of MMP-2 24,25 . EGCG can also inhibit the activation of MMP-8 26 , which in turn was shown to affect the remineralisation of artificially demineralised dentin 27 .…”
mentioning
confidence: 99%