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.
J Biochem Mol Toxicol. 2011 Nov-Dec;25(6):362-8. doi: 10.1002/jbt.20400. Epub 2011 Jul 28.
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.
采用荧光光谱法、圆二色光谱（CD 谱）和紫外-可见吸收光谱法研究了牛血清白蛋白（BSA）与 2-萘胺（2-NA）在水溶液中的相互作用机制。荧光光谱证明，2-NA 对 BSA 的荧光猝灭是 2-NA 与 BSA 形成复合物的结果，并根据改进的 Stern-Volmer 方程确定了 2-NA 在 BSA 中的结合常数（K(a)）和结合位点数。同步荧光和 CD 光谱的结果表明，2-NA 可以减少 BSA 的α-螺旋含量，导致蛋白质骨架的松动。紫外-可见吸收光谱和共振光散射光谱（RLS）的结果也表明，BSA 的构象发生了变化，发生了聚集，这可能对生物体产生毒性作用。
