| 离子型表面活性剂与牛血清白蛋白作用的比较研究 |
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| 引用本文： | 文 丰,王 芸,胡晓熙,岑光龙,张艳军,尹艳镇.离子型表面活性剂与牛血清白蛋白作用的比较研究[J].日用化学工业,2018,48(12):665-674. |
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| 作者姓名： | 文 丰 王 芸 胡晓熙 岑光龙 张艳军 尹艳镇 |
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| 作者单位： | 广西大学 化学化工学院，广西 南宁 530003 |
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| 基金项目： | 国家自然科学基金资助项目(51203082)；中国博士后科学基金资助项目(2014M552287)；广西自然科学基金杰出青年基金资助项目(2017GXNSFFA198007)；广西自然科学基金资助项目(2017GXNSFBA1980083)；广西高校化学工艺重点学科基金资助项目(2015KLOG16)；大学生创新创业训练计划项目资助(201811607025) |
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| 摘 要： | 采用荧光光谱、紫外吸收光谱、动态光散射和Zeta电位法对比研究了十二烷基硫酸钠(SDS)和十二烷基三甲基溴化铵(DTAB)与牛血清白蛋白(BSA)的相互作用机理。结果表明：SDS和DTAB均能猝灭BSA内源荧光，298 K时的猝灭常数Ksv分别为2.64×104和304.21 L/mol。同步荧光光谱和三维荧光光谱显示SDS和DTAB对BSA的构象产生了影响。SDS对BSA荧光猝灭机理为动静联合猝灭机制；热力学计算表明，SDS与BSA的结合过程中，静电力起主导作用，并且能与BSA形成SDS/BSA超分子复合物；DTAB对BSA荧光猝灭机理为动态猝灭，作用力主要是疏水作用。SDS和DTAB与BSA的平均结合距离分别为2.77和4.73 nm。综合结合常数、粒径和Zeta电位等变化，在相同条件下具有较大电荷密度和较小体积极性头基的SDS与BSA具有更强的结合作用。
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| 关 键 词： | 表面活性剂 牛血清白蛋白 荧光猝灭 比较研究 |
| 收稿时间： | 2018/6/13 0:00:00 |
Comparative study on the interactions between ionic surfactants and bovine serum albumin |
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| WEN Feng,WANG Yun,HU Xiao-xi,CEN Guang-long,ZHANG Yan-jun and YIN Yan-zhen.Comparative study on the interactions between ionic surfactants and bovine serum albumin[J].China Surfactant Detergent & Cosmetics,2018,48(12):665-674. |
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| Authors: | WEN Feng WANG Yun HU Xiao-xi CEN Guang-long ZHANG Yan-jun and YIN Yan-zhen |
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| Affiliation: | School of Chemistry & Chemical Engineering, Guangxi University, Nanning, Guangxi 530003, China |
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| Abstract: | A comparative study between two ionic surfactants, namely sodium dodecyl sulfate (SDS) and dodecyltrimethylammonium bromide (DTAB), for their interactions with bovine serum albumin (BSA) has been made by measurement of fluorescence, ultraviolet absorption, dynamic light scattering and Zeta potential. The results show that, both SDS and DTAB can quench the intrinsic fluorescence of BSA. The quenching constants Ksv at 298 K are 2.64×104 and 304.21 L/mol, respectively. Synchronous fluorescence spectra and three-dimensional fluorescence spectra show that SDS and DTAB have influences on the conformation of BSA. The fluorescence quenching of BSA by SDS occurs through a mixed static and dynamic quenching mechanism. The thermodynamic parameters reveal that the electrostatic force dominates in the formation of the SDS/BSA complex; DTAB can quench the intrinsic fluorescence of BSA by dynamic quenching, in which the hydrophobic force is dominating. The average binding distance of SDS and DTAB to BSA are calculated to be 2.77 and 4.73 nm. With the combination of results of binding constants, particle size and Zeta potential, it can be concluded that SDS with smaller polar headgroup and larger charge density has stronger binding to BSA under the same conditions. |
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| Keywords: | surfactant bovine serum albumin fluorescence quenching comparative study |
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