The interaction between cholesterol and human serum albumin.
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 = 3.84 nm. UV-vis spectra showed HSA molecules unfolded to some extent and the hydrophobicity was decreased in the presence of cholesterol.
Peng
Liu
L
School of Sciences, Wuhan University of Technology, Wuhan 430070, China. chemliup@whut.edu.cn
Minbo
He
H
Fang
Chen
C
Xi
Li
L
Chaocan
Zhang
Z
D001665:Binding Sites; D002784:Cholesterol / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D011487:Protein Conformation; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism*; D013816:Thermodynamics
D012709:Serum Albumin; D002784:Cholesterol