5,7,4′-三羟基取代黄酮化合物与牛血清白蛋白的相互作用  

Interaction of bovine serum albumin with 5,7,4′-trihydroxy substituent flavonoids

作　　者：王琳琳[1] 朱靖博[1,2] 寇自农[3] 丁燕[1,2] 杨荣荣[1] 

机构地区：[1]大连工业大学食品学院,辽宁大连116034 [2]大连工业大学植物资源化学与应用研究所,辽宁大连116034 [3]大连工业大学实验仪器中心,辽宁大连116034

出　　处：《大连工业大学学报》2015年第5期320-325,共6页Journal of Dalian Polytechnic University

基　　金：辽宁省高等学校重大科技平台项目(2011191)

摘　　要：利用荧光光谱法与紫外光谱法研究5,7,4′-三羟基取代类黄酮化合物芹菜素、柚皮素和染料木素与牛血清白蛋白(BSA)的结合,探讨了C环氢化及取代位置对其与BSA相互作用的影响。结果表明,3种化合物对BSA内源性荧光均有猝灭作用,且猝灭类型为静态猝灭;3种化合物与BSA的结合位点约为1,在295K条件下,与BSA结合由强到弱顺序为芹菜素、染料木素、柚皮素,结合常数分别为1.269×107、3.011×105和1.342×105 L/mol;芹菜素主要通过氢键与范德华力与BSA结合,柚皮素和染料木素主要通过静电作用与BSA结合;说明具有相同A环与B环结构的黄酮化合物,C环氢化后削弱其与BSA的作用,B环连接在C-2位置上与BSA的结合作用更强。3种化合物的加入均改变了BSA酪氨酸残基与色氨酸残基的微环境;同时也改变了蛋白质的二级结构与氨基酸残基,与BSA均形成了复合物。The interactions among 5,7,4′-trihydroxy substituent flavonoids apigenin,naringenin,genistein and bovine serum albumin（BSA）were investigated by fluorescence spectroscopy and ultraviolet spectroscopy.The effect of hydrogenation on C ring and the position of substituent on C ring on the affinity for BSA was discussed.Experimental results showed that the three flavonoids could quench BSA fluorescence and the quenching mechanism was static quenching.The binding numbers were all about 1.The descending order of binding force was apigenin（flavone）,genistein（flavanone）and naringenin（isoflavone）,the binding constant of which were 1.269×107,3.011×105and 1.342×105 L/mol at 295 K.The binding force between apigenin and BSA was mainly hydrogen bonding and van der Waals force,naringenin and genistein＇s were both electrostatic interaction.The results indicated that hydrogenation on ring C could lower the affinity to BSA,while the B ring connected to the C-2position could enhance the affinity to BSA.The three flavonoids changed the microenvironment of tyrosine and tryptophan.The three flavonoids were formed compound with BSA,and also changed the protein secondary structure and amino acid residues microenvironment.

关 键 词：5 7 4′-三羟基取代黄酮化合物 芹菜素 柚皮素 染料木素 牛血清白蛋白 荧光光谱法 紫外光谱法 

分 类 号：O657.3[理学—分析化学]