albumin - publications

Predict more albumin - ligand interactions now!


1. Food Chem Toxicol. 2012 Apr 16. [Epub ahead of print]

Multiple spectroscopic studies on the interaction between olaquindox, a feed
additive, and bovine serum albumin.

Xu T, Guo X, Zhang L, Pan F, Lv J, Zhang Y, Jin H.

College of Chemistry, Liaoning University, 66 Chongshan Middle Road, Shenyang
110036, People's Republic of China.

The interaction between olaquindox (OLA) and bovine serum albumin (BSA) was
investigated using fluorescence, UV-vis absorption and circular dichroism (CD)
spectroscopy. The results showed that the fluorescence quenching of BSA by OLA
was a static quenching process induced by the formation of OLA-BSA complex. The
binding constant of OLA-BSA complex was calculated to be 1.299×104Lmol(-1)
(293K). The negative values of ΔH(0) and ΔS(0) indicated that hydrogen bond and
van der Waals interactions played major roles in stabilizing the complex. Site
probe competition experiments and number of binding sites (n) revealed that OLA
could bind to site I in subdomain IIA of BSA, and the binding distance (r) was
evaluated to be 3.643nm according to Förster's non-radiative energy transfer
theory. The results of CD and three-dimensional fluorescence spectra suggested
some conformational changes of BSA after OLA binding.

Copyright © 2012. Published by Elsevier Ltd.

PMID: 22525866 [PubMed - as supplied by publisher]