Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/12990
Title: Studies on the binding of isoalantolactone to human serum albumin by molecular spectroscopy and modeling
Authors: Sun, Yang
Hu, Chun-Mei
Li, Guo-Bo
Yang, Sheng-Yong
Liu, Lu-Sha
Tan, Chun-Lei
Wei, Song
Hu, Xiao-Yun
Zhao, Ying-Yong
Fan, Jun
Keywords: Bioinorganic chemistry
Isoalantolactone
Human serum albumin
Fluorescence spectroscopy
Molecular modelling
Binding sites
Issue Date: Nov-2011
Publisher: NISCAIR-CSIR, India
Abstract: The interactions between isoalantolactone (IAL) and human serum albumin (HSA) under simulative physiological conditions have been investigated by fluorescence, absorption and circular dichroism spectra. Fluorescence data reveal that the fluorescence quenching of HSA by IAL is the result of formation of the IAL–HSA complex. The thermodynamic parameters, enthalpy change and entropy change for the reaction are calculated to be -34.317 kJ mol–1 and -7.522 J mol–1 K–1, respectively, indicating that the hydrogen bonds and hydrophobic interactions play a dominant role in the binding of IAL to HSA. The conformational investigation shows that the presence of IAL decreases the -helical content of HSA and induces the remarkable unfolding of the polypeptides of protein. Furthermore, displacement experiments using warfarin and ibuprofen indicate that IAL could bind to site I of HSA, which is in agreement with the results obtained from molecular modeling.
Description: 1547-1554
URI: http://hdl.handle.net/123456789/12990
ISSN: 0975-0975(Online); 0376-4710(Print)
Appears in Collections:IJC-A Vol.50A(11) [November 2011]

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