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Gemini 表面活性剂 14-6-14 与牛血清白蛋白相互作用的荧光光谱研究。

Fluorescence spectroscopic studies on the interaction of Gemini surfactant 14-6-14 with bovine serum albumin.

机构信息

Ministry of Education Key Laboratory for the Synthesis and Application of Organic Function Molecules, Hubei University, Wuhan 430062, People's Republic of China.

出版信息

Luminescence. 2012 May-Jun;27(3):204-10. doi: 10.1002/bio.1333. Epub 2011 Jul 14.

DOI:10.1002/bio.1333
PMID:21755587
Abstract

The interaction of the cationic Gemini surfactant hexamethylene-1,3-bis (tetradecyldimethylammonium bromide) (14-6-14) with bovine serum albumin (BSA) has been investigated by fluorescence quenching spectra and three-dimensional (3D) fluorescence spectra. The Stern-Volmer quenching constants K(SV) and the corresponding thermodynamic parameters ΔH, ΔG and ΔS have been estimated by the fluorescence quenching method. The results indicated that hydrophobic forces were the predominant intermolecular forces between BSA and the surfactant. Competitive experiments and the number of binding sites calculation show that 14-6-14 can be inserted in site-II (in subdomain IIIA) of BSA. The effect of 14-6-14 on the conformation of BSA was evaluated by synchronous fluorescence spectroscopy and 3D fluorescence spectral methods. The results show that the conformation of BSA was changed dramatically in the presence of 14-6-14, by binding to the Trp and Try residues of BSA. The investigation provides interaction between BSA and 14-6-14 as a model for molecular design and industrial research.

摘要

通过荧光猝灭光谱和三维(3D)荧光光谱研究了阳离子双子表面活性剂十六烷-1,3-双(十四烷基二甲基溴化铵)(14-6-14)与牛血清白蛋白(BSA)的相互作用。通过荧光猝灭法估算了 Stern-Volmer 猝灭常数 K(SV)和相应的热力学参数ΔH、ΔG 和ΔS。结果表明,BSA 与表面活性剂之间主要存在疏水相互作用力。竞争实验和结合位点数计算表明,14-6-14 可以插入 BSA 的 II 型结合位(亚域 IIIA)。通过同步荧光光谱和 3D 荧光光谱法评价了 14-6-14 对 BSA 构象的影响。结果表明,14-6-14 的存在使 BSA 的构象发生了显著变化,与 BSA 的色氨酸和酪氨酸残基结合。该研究为分子设计和工业研究提供了 BSA 与 14-6-14 相互作用的模型。

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