Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9890839 | International Journal of Biological Macromolecules | 2005 | 5 Pages |
Abstract
We investigated the interaction between colchicine and human serum albumin (HSA) by fluorescence and UV-vis absorption spectroscopy. In the mechanism discussion, it was proved that the fluorescence quenching of HSA by colchicine is a result of the formation of colchicines-HSA complex; van der Waals interactions and hydrogen bonds play a major role in stabilizing the complex. The modified Stern-Volmer quenching constant Ka and corresponding thermodynamic parameters ÎH, ÎG, ÎS at different temperatures were calculated. The distance r between donor (Trp214) and acceptor (colchicine) was obtained according to fluorescence resonance energy transfer (FRET).
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Biochemistry
Authors
Yan-Jun Hu, Yi Liu, Ru-Ming Zhao, Song-Sheng Qu,