光谱法和分子对接研究高儿茶酚与牛血清白蛋白的相互作用
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(1.渤海大学食品科学与工程学院 辽宁锦州 121013;2.上海交通大学农业与生物学院 上海 200240)

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辽宁省食品安全重点实验室开放课题(LNKLFS202104);辽宁省兴辽英才计划项目(XLYC1807133)


Studies on the Interaction between Homocatechol and Bovine Serum Albumin Using Spectroscopic and Molecular Docking
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(1.College of Food Science and Technology, Bohai University, Jinzhou 121013, Liaoning;2.School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai 200240)

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    摘要:

    对高儿茶酚与牛血清白蛋白(BSA)相互作用进行研究,结果表明:高儿茶酚能猝灭BSA的荧光;与BSA主要通过疏水键自发形成具有弱荧光的大分子复合物,且高儿茶酚在BSA上至少存在一个结合位点;在298,310 K和320 K时,高儿茶酚与BSA的结合常数Ka分别为5.908×102,5.424×104,1.535×106 L/mol。推测高儿茶酚对BSA的猝灭是以动态猝灭为主,也有静态猝灭过程。冷场发射扫描电镜观察发现,添加2 μmol/L的高儿茶酚,可以促进蛋白质的溶解,使其分布更加均匀;当高儿茶酚浓度高于2 μmol/L时,使蛋白质发生聚集。分子对接分析发现,高儿茶酚主要通过疏水键、氢键和范德华力稳定地结合在BSA亚结构域ⅡA的疏水口袋中(siteⅠ)。

    Abstract:

    The interaction between homocatechol and bovine serum albumin(BSA) was studied. The results showed that homocatechol could quench the fluorescence of BSA. A macromolecular complex with weak fluorescence was spontaneously formed with BSA mainly through hydrophobic bond, and at least one binding site of homocatechol on BSA at 298, 310 K and 320 K. The binding constants of homocatechol to BSA were 5.908×102, 5.424×104, 1.535×106 L/mol. It is speculated that the quenching of BSA by homocatechol was mainly dynamic quenching, and there is also a static quenching process. The cold field emission scanning electron microscopy showed that 2 μmol/L homocatechol could promote the dissolution of protein and made its distribution more uniform. When the concentration of homocatechol was 2 μmol/L, the protein would aggregate. Molecular docking analysis showed that homocatechol was stably bound to the hydrophobic pocket of BSA Subdomain IIA (site I) mainly through hydrophobic bond, hydrogen bond and van der Waals force.

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吕艳芳,张紫卿,梁倩倩,李营,刘欣欣,李学鹏.光谱法和分子对接研究高儿茶酚与牛血清白蛋白的相互作用[J].中国食品学报,2022,22(12):72-81

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  • 收稿日期:2021-12-13
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  • 在线发布日期: 2023-01-09
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