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作 者:于湛[1,2] 何妍[1] 戚涵姝 谷笑雨 刘丽艳[1] 苏桂田[1] 辛士刚[3] YU Zhan HE Yan QI Hanshu GU Xiaoyu LIU Liyan SU Guitian XIN Shigang(School of Chemistry and Chemical Engineering, Shenyang Normal University, Shenyang 110034, China Experimental Center, Shenyang Normal University, Shenyang 110034, China Provincial Key Laboratory for Separation and Analysis of Complex Systems in Liaoning Universities, Shenyang Normal University, Shenyang 110034, China)
机构地区:[1]沈阳师范大学化学化工学院,沈阳110034 [2]沈阳师范大学复杂体系分离与分析辽宁省高校重点实验室,沈阳110034 [3]沈阳师范大学实验中心,沈阳110034
出 处:《沈阳师范大学学报(自然科学版)》2017年第2期208-213,共6页Journal of Shenyang Normal University:Natural Science Edition
基 金:国家自然科学基金资助项目(21205080);教育部留学回国人员科研启动基金(教外司留[2012]1707);辽宁省高等学校优秀人才支持计划(LJQ2015105)
摘 要:利用荧光光谱法以及分子对接计算研究了橙皮素同人血清白蛋白(HSA)间的相互作用,并将结果同牛血清白蛋白(BSA)进行对比。实验结果表明,橙皮素均可以通过静态猝灭的方式有效地猝灭这2种蛋白质,且猝灭常数相近,猝灭效率差别很小。橙皮素与HSA结合位点数与BSA相同,但是结合常数小于BSA,并且同步荧光光谱数据显示橙皮素与BSA和HSA的相互作用使得这2种血清蛋白的结构发生了一些变化,从而导致荧光猝灭。分子对接计算表明,橙皮素同BSA及HSA的作用方式相似,都是在疏水及氢键作用驱动下结合在BSA或HSA部分氨基酸残基形成的疏水性口袋中。The interaction between hesperetin and human serum albumin(HSA)was investigated in this work,contrasted with the interaction between hesperetin and bovine serum albumin(BSA),by the method of fluorescence spectroscopy and molecular docking simulation.Experimental results show that the fluorescence of both BSA and HSA can be effectively quenched by the addition of hesperetin due to the static quenching mechanism.The quenching constants for the two proteins are similar and quenching efficiency are also alike.The numbers of binding sites of hesperetin to BSA and HSA are same but the binding constant of hesperetin and HSA are smaller than that of BSA.Synchronous fluorescence study indicates that the presence of hesperetin leads to slightly structural changes of proteins which causes fluorescence quenching of BSA and HSA.Molecular docking simulation shows that hydrophobic interactions and hydrogen bonding drive BSA and HSA to include hesperetin in their hydrophobic pockets formed by some amino acid residues of theirs.
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