E-resources
Peer reviewed
-
Mozzicafreddo, M.; Cuccioloni, M.; Eleuteri, A.M.; Fioretti, E.; Angeletti, M.
Biochimie, September 2006, 2006-Sep, 2006-09-00, 20060901, Volume: 88, Issue: 9Journal Article
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.
