Abstract
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.
Keywords: Cholesterol, quenching, thermodynamic parameter, hydrophobicity
Protein & Peptide Letters
Title: The Interaction Between Cholesterol and Human Serum Albumin
Volume: 15 Issue: 4
Author(s): Liu Peng, He Minbo, Chen Fang, Li Xi and Zhang Chaocan
Affiliation:
Keywords: Cholesterol, quenching, thermodynamic parameter, hydrophobicity
Abstract: 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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Cite this article as:
Peng Liu, Minbo He, Fang Chen, Xi Li and Chaocan Zhang, The Interaction Between Cholesterol and Human Serum Albumin, Protein & Peptide Letters 2008; 15(4) . https://dx.doi.org/10.2174/092986608784246542
DOI https://dx.doi.org/10.2174/092986608784246542 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |

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