Journal
PROTEIN AND PEPTIDE LETTERS
Volume 15, Issue 4, Pages 360-364Publisher
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/092986608784246542
Keywords
cholesterol; quenching; thermodynamic parameter; hydrophobicity
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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.
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