物理化学学报 >> 2016, Vol. 32 >> Issue (12): 2951-2960.doi: 10.3866/PKU.WHXB201609231

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季铵盐型阳离子表面活性剂与牛血清白蛋白的相互作用

谢湖均1,*(),刘程程1,孙强1,顾青2,*(),雷群芳3,方文军3,*()   

  1. 1 浙江工商大学应用化学系,杭州310018
    2 浙江工商大学食品与生物工程学院,杭州310018
    3 浙江大学化学系,杭州310028
  • 收稿日期:2016-07-18 发布日期:2016-11-30
  • 通讯作者: 谢湖均,顾青,方文军 E-mail:hujunxie@gmail.com;guqing2002@hotamail.com;fwjun@zju.edu.cn
  • 基金资助:
    国家自然科学基金(21203166，21473157);浙江省自然科学基金(LY16B030001);与浙江省重中之重学科食品科学与工程(JYTsp2014111)

The Interactions between Quaternary Ammonium Cationic Surfactants and Bovine Serum Albumin

Hu-Jun XIE1,*(),Cheng-Cheng LIU1,Qiang SUN1,Qing GU2,*(),Qun-Fang LEI3,Wen-Jun FANG3,*()   

  1. 1 Department of Applied Chemistry, Zhejiang Gongshang University, Hangzhou 310018, P. R. China
    2 School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, P. R. China
    3 Department of Chemistry, Zhejiang University, Hangzhou 310028, P. R. China
  • Received:2016-07-18 Published:2016-11-30
  • Contact: Hu-Jun XIE,Qing GU,Wen-Jun FANG E-mail:hujunxie@gmail.com;guqing2002@hotamail.com;fwjun@zju.edu.cn
  • Supported by:
    The project was supported by the National Natural Science Foundation of China(21203166，21473157);Natural Science Foundation of ZhejiangProvince, China(LY16B030001);and Food Science and Engineering the Most Important Discipline of Zhejiang Province, China(JYTsp2014111)

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摘要：

本文合成并表征了三种不同烷基链长度的季铵盐型阳离子表面活性剂：N-十二烷基-N-（2-羟乙基）-N，N-二甲基溴化铵（DHDAB）、N-十四烷基-N-（2-羟乙基）-N，N-二甲基溴化铵（THDAB）、N-十六烷基-N-（2-羟乙基）-N，N-二甲基溴化铵（CHDAB）。采用荧光光谱法、紫外-可见光谱法、动态光散射法和等温滴定量热法对三种表面活性剂与牛血清白蛋白（BSA）的相互作用进行研究。荧光光谱研究表明，三种表面活性剂主要与BSA分子内的色氨酸残基发生相互作用，导致蛋白质的构象发生变化，且表面活性剂烷基链越长，与BSA的相互作用就越强。BSA荧光猝灭的主要原因是静态猝灭，紫外光谱实验同样验证了静态猝灭的存在。等温滴定量热法结果表明低浓度的表面活性剂与BSA主要发生静电作用和疏水作用而放热。动态光散射结果表明高浓度的表面活性剂会使BSA结构被破坏。本文揭示了表面活性剂与BSA相互作用的机理，为表面活性剂的广泛应用提供了理论基础。

关键词: 表面活性剂, 牛血清白蛋白, 荧光猝灭, 动态光散射, 等温滴定量热

Abstract:

UV-visible (UV-Vis) absorption spectroscopy, fluorescence spectroscopy (FL), dynamic light scattering (DLS) and isothermal titration calorimetry (ITC) were used to study the interactions between bovine serum albumin (BSA) and the three quaternary ammonium surfactants N-dodecyl-N-(2-hydroxyethyl)-N, Ndimethyl ammonium bromide (DHDAB), N-tetradecyl-N-(2-hydroxyethyl)-N, N-dimethyl ammonium bromide (THDAB) and N-cetyl-N-(2-hydroxyethyl)-N, N-dimethyl ammonium bromide (CHDAB). These surfactants quenched the intrinsic fluorescence of BSA, with longer alkyl chains resulting in more significant quenching. This was attributed to static quenching. Further evidence of static quenching was provided by UV-Vis absorption spectroscopy. The particle size of BSA was found to initially increase and then decrease with increasing surfactant concentration. The concentration of surfactant changed the type of interaction mode. This work revealed the mechanism and binding characteristics between surfactants and protein, and provides the basis for further applications of surfactants.

Key words: Surfactants, Bovine serum albumin, Fluorescence quenching, Dynamic light scattering, Isothermal titration calorimetry