Spectroscopic investigation of the interaction of the toxicant, 2-naphthylamine, with bovine serum albumin

✍ Scribed by Yan Liu; Mingmao Chen; Guangling Bian; Junfeng Liu; Ling Song

• Publisher: John Wiley and Sons
• Year: 2011
• Tongue: English
• Weight: 269 KB
• Volume: 25
• Category: Article
• ISSN: 1095-6670
• DOI: 10.1002/jbt.20400

✦ Synopsis

Abstract

The mechanism of interaction between bovine serum albumin (BSA) and 2‐naphthylamine (2‐NA) in aqueous solution was investigated by fluorescence spectroscopy, circular dichroism (CD) spectra, and UV–vis spectroscopy. It was proved from fluorescence spectra that the fluorescence quenching of BSA by 2‐NA was a result of the formation of complex between 2‐NA and BSA, and the binding constants (K~a~) as well as the numbers of binding sites for 2‐NA in BSA were determined according to the modified Stern–Volmer equation. The results of synchronous fluorescence and CD spectra demonstrated 2‐NA could decrease the amount of α‐helix of BSA, leading to the loosening of protein skeleton. UV–vis spectroscopy and resonance light scattering spectra (RLS) results also suggested the conformation of BSA were changed and the BSA aggregation occured, which could induce toxic effects on the organism. © 2011 Wiley Periodicals, Inc. J Biochem Mol Toxicol 25:362–368 2011; View this article online at wileyonlinelibrary.com. DOI 10.1002/jbt.20400