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Investigation of the Interaction between Adenosine and Human Serum Albumin by Fluorescent Spectroscopy and Molecular Modeling
Author(s) -
CUI FengLing,
WANG JunLi,
LI Fang,
FAN Jing,
QU GuiRong,
YAO XiaoJun,
LEI BeiLei
Publication year - 2008
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.200890125
Subject(s) - chemistry , human serum albumin , quenching (fluorescence) , enthalpy , fluorescence , fluorescence spectroscopy , intermolecular force , molecular model , hydrophobic effect , spectroscopy , molecular dynamics , entropy (arrow of time) , thermodynamics , analytical chemistry (journal) , computational chemistry , molecule , chromatography , stereochemistry , organic chemistry , quantum mechanics , physics
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.