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

Authors

  • Yan Liu,

    1. 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
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  • Mingmao Chen,

    1. Department of Biomaterials & Artificial Organ, Institute of Biomedical Engineering, Chinese Academy of Medical Science & Peking Union Medical College, Key Laboratory of Biomedical Material of Tianjin, Tianjin 300192, People's Republic of China
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  • Guangling Bian,

    1. 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
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  • Junfeng Liu,

    1. 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
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  • Ling Song

    Corresponding author
    1. 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
    • 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
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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 (Ka) 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

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