| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5402079 | Journal of Luminescence | 2011 | 8 Pages |
Abstract
⺠We investigate the binding mechanism of vitexin to human serum albumin (HSA) by different multi-spectroscopic techniques under simulated physiological conditions. ⺠Vitexin can strongly quench the ï¬uorescence of HSA through a static quenching mechanism. ⺠The interaction of vitexin with HSA is driven mainly by hydrogen bond and van der Waals forces. ⺠The binding distance between HSA and vitexin is 4.16 nm, and vitexin is mainly located in the region of site I (subdomain IIA). ⺠The binding of vitexin to HSA can induce conformational changes of HSA.
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Authors
Guowen Zhang, Nan Zhao, Lin Wang,