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Investigation of the Interaction between Adenosine and Human Serum Albumin by Fluorescent Spectroscopy and Molecular Modeling

✍ Scribed by Feng-Ling CUI; Jun-Li WANG; Fang LI; Jing FAN; Gui-Rong QU; Xiao-Jun YAO; Bei-Lei LEI

Publisher: John Wiley and Sons
Year: 2008
Tongue: English
Weight: 111 KB
Volume: 26
Category: Article
ISSN: 0256-7660
DOI: 10.1002/cjoc.200890125

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✦ Synopsis

Abstract

The binding interaction of adenosine with human serum albumin (HSA) was investigated under simulative physiological conditions by fluorescence spectroscopy in combination with a molecular modeling method. A strong fluorescence quenching reaction of adenosine to HSA was observed and the quenching mechanism was suggested as static quenching according to the Stern‐Volmer equation. The binding constants (K) at different temperatures as well as thermodynamic parameters, enthalpy change (Δ__H__) and entropy change (Δ__S__), were calculated according to relevant fluorescent data and Vant′Hoff equation. The hydrophobic interaction was a predominant intermolecular force in order to stabilize the complex, which was in agreement with the results of molecular modeling study.

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