| Literature DB >> 16690199 |
M Mozzicafreddo1, M Cuccioloni, A M Eleuteri, E Fioretti, M Angeletti.
Abstract
The effect of a group of natural flavonoids on human thrombin amidolytic activity was investigated using a spectrophotometric inhibition assay while information on the kinetics and thermodynamics was obtained using optical biosensor techniques. All the flavonoids tested acted as reversible inhibitors, and the quercetin-thrombin complex was found to be most stable at pH=7.5. Docking analysis indicated that quercetin's inhibitory behavior could be related to its planar structure and low steric hindrance, and to its ability to form a critical H-bond with thrombin His57.Entities:
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Year: 2006 PMID： 16690199 DOI： 10.1016/j.biochi.2006.04.007
Source DB: PubMed Journal: Biochimie ISSN： 0300-9084 Impact factor: 4.079