N-酰基氨基酸型表面活性剂与牛血清蛋白相互作用研究  

Study on the interaction between N-acyl amino acid surfactants and bovine serum albumi

作　　者：惠蒙蒙 张晨龙 杨许召 白亚榕 王军 HUI Meng-meng;ZHANG Chen-long;YANG Xu-zhao;BAI Ya-rong;WANG Jun(Zhengzhou University of Light Industry,Zhengzhou,Henan 450002,China)

机构地区：[1]郑州轻工业大学,河南郑州450002

出　　处：《日用化学工业》2020年第9期596-602,623,共8页China Surfactant Detergent & Cosmetics

基　　金：“十二五”国家科技支撑计划资助项目(2013BAC01B04);河南省科技攻关项目(162102210056)。

摘　　要：通过荧光光谱和紫外吸收光谱研究了牛血清蛋白(BSA)与N-月桂酰基肌氨酸钠(SLS)、N-月桂酰基谷氨酸钠(SLGLU)和N-月桂酰基甘氨酸钠(SLG) 3种N-酰基氨基酸型表面活性剂之间的相互作用。随着3种表面活性剂浓度增加,BSA中色氨酸残基的内源荧光光谱波长都发生了蓝移,色氨酸残基所处微环境极性减弱。荧光探针法测得3种表面活性剂在蛋白质表面上形成聚集体所需的临界浓度(cac)分别为:cacSLS=0.4 mmol/L,cacSLG=0.1 mmol/L,cacSLGLU=0.09 mmol/L。BSA与3种表面活性剂相互作用的结合等温线基本上都可以划分为特异性结合、非协同结合、协同结合和饱和4个特征区域。随着表面活性剂浓度增大,BSA中色氨酸残基的紫外特征吸收波长红移,氨基酸残基所处微环境极性减弱,而酪氨酸和苯丙氨酸残基的紫外特征吸收波长蓝移,氨基酸残基所处微环境极性增强。利用苯基丁氮酮、布洛芬、氯化血红素探针分析,确定了3种表面活性剂与BSA相互作用时的结合位点为BSA结构域ⅡA的Trp-213附近位置,并对不同表面活性剂浓度时AAS与BSA相互作用方式进行了分析。The interaction between bovine serum albumi(BSA)and three N-acyl amino acid surfactants,including sodium lauroyl sarcosinate(SLS),sodium lauroyl glutamate(SLGLU)and sodium lauroyl glycine(SLG)was studied by fluorescence spectrum and UV spectrum in this paper.The fluorescence peak wavelength of tryptophan residue in BSA showed a blue-shift with the increase of the concentration of the three surfactants,and the polarity of microenvironment around the tryptophan residue was decreased.The critical aggregation concentrations(cac)of the three surfactants on protein surface of BSA by fluorescence spectrum are:cac SLS=0.4 mmol/L,cac SLG=0.1 mmol/L,and cac SLGLU=0.09 mmol/L,respectively.The binding isotherms of BSA interacted with the three surfactants can be divided into four feature regions:specific binding,non-cooperative binding,cooperative binding and saturation.With the increase of surfactant concentration,the characteristic UV absorption wavelength of tryptophan residue in BSA is red shifted,and the polarity of amino acid residues in the microenvironment is decreased;while the characteristic UV absorption wavelengths of tyrosine and phenylalanine residues in BSA are blue-shift,and the polarity of amino acid residues in BSA is enhanced.The binding site of BSA with the three surfactants was confirmed at the vicinity of Trp-213 of BSA domain II A by probe molecules,such as phenylbutazone,ibuprofen and heme chloride.The interaction modes between AAS and BSA at different surfactant concentrations were analyzed.

关 键 词：表面活性剂 牛血清蛋白 氨基酸 相互作用 荧光光谱 

分 类 号：TQ423[化学工程]