albumin - publications

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1. Spectrochim Acta A Mol Biomol Spectrosc. 2012 Mar 3. [Epub ahead of print]

Spectroscopic studies on the interaction of bovine serum albumin with surfactants
and apigenin.

Zhao XN, Liu Y, Niu LY, Zhao CP.

Experimental Center, Henan Institute of Science and Technology, Xinxiang 453003,
PR China.

The binding of apigenin (Ap) to bovine serum albumin (BSA) has been studied using
the methods of fluorescence spectroscopy and UV-vis absorption spectroscopy. The
spectroscopic analysis of the quenching mechanism indicates that the quenching
constants are inversely correlated with the temperatures and the quenching
process could result from a static interaction. The type of interaction force was
discussed and the binding site of Ap was in site I (subdomain IIA) of BSA. The
thermodynamic parameters ΔH and ΔS are -42.02kJmol(-1) and -48.31Jmol(-1)K(-1),
respectively and the negative ΔG implying that the binding interaction was
spontaneous. The distance r between BSA and Ap was calculated according to
Förster's theory and the value is 3.44nm. The synchronous and three-dimensional
fluorescence spectra show that the binding of Ap to BSA could lead to the changes
in the conformation and microenvironment of BSA. At the same time, the effects of
ionic surfactants on the interaction of Ap and BSA have also been investigated.

Copyright © 2012. Published by Elsevier B.V.

PMID: 22561754 [PubMed - as supplied by publisher]