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Journal of Chemistry
Volume 2013, Article ID 308054, 6 pages
http://dx.doi.org/10.1155/2013/308054
Research Article

Fluorescence Spectroscopy Study on the Interaction between Evodiamine and Bovine Serum Albumin

1School of Chemistry and Material, Yulin Normal University, Yulin 537000, China
2The Key Laboratory for the Chemistry and Molecular Engineering of Medicinal Resources, School of Chemistry & Chemical Engineering, Guangxi Normal University, Guilin 541004, China

Received 14 June 2012; Accepted 3 December 2012

Academic Editor: Tomokazu Yoshimura

Copyright © 2012 Mingxiong Tan et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

The interaction of evodiamine (Evo) with bovine serum albumins (BSAs) at different two temperatures (298 and 310?K) was investigated by means of fluorescence spectroscopy. The experimental results showed that Evo binds with BSA via a static quenching procedure with association constants of ?L/mol at 298?K and ?L/mol at 310?K. The number of bound Evo molecules per protein is 1.31 at 298?K and 1.33 at 310?K. The results suggested that Evo reacts with BSA chiefly through hydrophobic and electrostatic interactions, and it does not alter the a-helical nature of BAS.