Interaction of colchicine with human serum albumin investigated by spectroscopic methods.
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 K(a) and corresponding thermodynamic parameters deltaH, deltaG, deltaS at different temperatures were calculated. The distance r between donor (Trp214) and acceptor (colchicine) was obtained according to fluorescence resonance energy transfer (FRET).
Hu
Yan-Jun
YJ
College of Chemistry and Molecular Sciences, Wuhan University, Wuhan 430072, PR China.
Liu
Yi
Y
Zhao
Ru-Ming
RM
Qu
Song-Sheng
SS
D001665:Binding Sites; D003078:Colchicine / Q000737:chemistry* / Q000494:pharmacology; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods; D006074:Gout Suppressants / Q000737:chemistry / Q000494:pharmacology; D006801:Humans; D006860:Hydrogen Bonding; D007700:Kinetics; D046911:Macromolecular Substances / Q000737:chemistry; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry*; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013053:Spectrophotometry; D013056:Spectrophotometry, Ultraviolet / Q000379:methods*; D013696:Temperature; D013816:Thermodynamics; D014466:Ultraviolet Rays
D006074:Gout Suppressants; D046911:Macromolecular Substances; D012709:Serum Albumin; D003078:Colchicine