A study on the interaction between 5-Methyluridine and human serum albumin using fluorescence quenching method and molecular modeling.
This work was designed to study the interaction between 5-Methyluridine and human serum albumin (HSA) under simulative physiological conditions using fluorescence spectroscopy in combination with molecular modeling technique for the first time. Static quenching was suggested by the fluorescence measurement. The binding constants (K) were calculated according to the relevant fluorescence data at different conditions including temperature. Thermodynamic parameter, different conditions including temperature to determine enthalpy change and entropy change, indicating the hydrophobic force played a major role in the binding interaction between 5-Methyluridine and HSA. The experimental result was in correspondence with molecular modeling theory.
Cui
Feng-Ling
FL
School of Chemistry and Environmental Science, Key Laboratory for Yellow River and Huai he River Water Environment and Pollution Control Ministry of Education, Henan Normal University, Xinxiang, People's Republic of China. cuifl718@hotmail.com
Yan
Ying-Hua
YH
Zhang
Qiang-Zhai
QZ
Qu
Gui-Rong
GR
Du
Juan
J
Yao
Xiao-Jun
XJ
D006801:Humans; D008722:Methods; D008958:Models, Molecular; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013696:Temperature; D013816:Thermodynamics; D014529:Uridine / Q000031:analogs & derivatives* / Q000737:chemistry
D012709:Serum Albumin; C009182:ribothymidine; D014529:Uridine