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Spectroscopic investigation of the interaction of the toxicant, 2‐naphthylamine, with bovine serum albumin
Author(s) -
Liu Yan,
Chen Mingmao,
Bian Guangling,
Liu Junfeng,
Song Ling
Publication year - 2011
Publication title -
journal of biochemical and molecular toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.526
H-Index - 58
eISSN - 1099-0461
pISSN - 1095-6670
DOI - 10.1002/jbt.20400
Subject(s) - bovine serum albumin , chemistry , circular dichroism , fluorescence spectroscopy , fluorescence , quenching (fluorescence) , spectroscopy , tryptophan , analytical chemistry (journal) , aqueous solution , serum albumin , crystallography , photochemistry , chromatography , biochemistry , amino acid , physics , quantum mechanics
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