Liu Peng, He Minbo, Chen Fang, Li Xi and Zhang Chaocan Pages 360 - 364 ( 5 )
The interaction between cholesterol and Human Serum Albumin (HSA) was studied by fluorescence technique. Addition of cholesterol causes decreasing of the fluorescence intensity of HSA and the mechanism can be attributed to static quenching. Both negative enthalpy and entropy change indicate this binding was an “enthalpy-driven” reaction. The number of binding site and distance between residues and ligands were also calculated: n=0.98, r=3.84nm. UV – vis spectra showed HSA molecules unfolded to some extent and the hydrophobicity was decreased in the presence of cholesterol.
Cholesterol, quenching, thermodynamic parameter, hydrophobicity
Department of Chemistry,School of Sciences, Wuhan University of Technology, Wuhan 430070, P.R.China.