title: Spectroscopic investigation of the interaction of the toxicant, 2-naphthylamine, with bovine serum albumin.
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.
authors.affiliation: The State Key Lab of Structural Chemistry, Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, Fuzhou, Fujian 350002, People's Republic of China.
authors.forename: Yan
authors.initials: Y
authors.lastname: Liu
authors.forename: Mingmao
authors.initials: M
authors.lastname: Chen
authors.forename: Guangling
authors.initials: G
authors.lastname: Bian
authors.forename: Junfeng
authors.initials: J
authors.lastname: Liu
authors.forename: Ling
authors.initials: L
authors.lastname: Song
mesh_terms: D015081:2-Naphthylamine / Q000737:chemistry* / Q000633:toxicity*; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002942:Circular Dichroism; D008027:Light; D011485:Protein Binding; D017433:Protein Structure, Secondary; D012542:Scattering, Radiation; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet
chemical_list: D012710:Serum Albumin, Bovine; D015081:2-Naphthylamine