• EI
  • Scopus
  • 食品科学与工程领域高质量科技期刊分级目录第一方阵T1
  • DOAJ
  • EBSCO
  • 北大核心期刊
  • 中国核心学术期刊RCCSE
  • JST China
  • FSTA
  • 中国精品科技期刊
  • 中国农业核心期刊
  • CA
  • WJCI
  • 中国科技核心期刊CSTPCD
  • 中国生物医学SinoMed
中国精品科技期刊2020
梁鑫富,董庆亮. 光谱法结合分子对接技术研究柠檬苦素与牛血清白蛋白的相互作用[J]. 华体会体育,2024,45(21):37−44. doi: 10.13386/j.issn1002-0306.2023100285.
引用本文: 梁鑫富,董庆亮. 光谱法结合分子对接技术研究柠檬苦素与牛血清白蛋白的相互作用[J]. 华体会体育,2024,45(21):37−44. doi: 10.13386/j.issn1002-0306.2023100285.
LIANG Xinfu, DONG Qingliang. Spectroscopic Method Combined with Molecular Docking Technique to Study the Interaction of Limonin with Bovine Serum Albumin[J]. Science and Technology of Food Industry, 2024, 45(21): 37−44. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2023100285.
Citation: LIANG Xinfu, DONG Qingliang. Spectroscopic Method Combined with Molecular Docking Technique to Study the Interaction of Limonin with Bovine Serum Albumin[J]. Science and Technology of Food Industry, 2024, 45(21): 37−44. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2023100285.

光谱法结合分子对接技术研究柠檬苦素与牛血清白蛋白的相互作用

Spectroscopic Method Combined with Molecular Docking Technique to Study the Interaction of Limonin with Bovine Serum Albumin

  • 摘要: 为研究柠檬苦素(Limonin,LM)与牛血清白蛋白(Bovine serum albumin,BSA)相互作用,本文采用紫外光谱法、荧光光谱法及分子对接技术研究LM与BSA的相互作用机制。结果表明:LM能有效淬灭BSA的内源荧光,其淬灭类型为静态淬灭;两者发生相互作用可形成1个结合位点,分子间作用力主要为氢键和范德华力,该相互作用过程为自发反应;紫外光谱及同步荧光光谱表明,LM与BSA发生相互作用后,可以增加BSA上酪氨酸(Tyr)、色氨酸(Trp)残基微环境的疏水性;通过竞争位点实验及分子对接,发现LM与BSA的结合位点在siteⅠ附近,LM可以与BSA上的Trp-213形成氢键,与Tyr-340/451等残基之间存在范德华力。

     

    Abstract: In order to study the interaction between limonin (LM) and bovine serum albumin (BSA), in this paper, the interaction mechanism between LM and BSA was explored by ultraviolet (UV) spectroscopy, fluorescence spectroscopy and molecular docking technology. The results showed that LM could significantly quench the endogenous fluorescence of BSA, displaying a static quenching type. In addition, LM formed a binding site with BSA by hydrogen bonding and van der Waals forces, demonstrating a spontaneous interaction mechanism. Meanwhile, UV spectroscopy and synchronous fluorescence spectroscopy showed that the interaction between LM and BSA could increase the hydrophobicity of tyrosine (Tyr) and tryptophan (Trp) residue microenvironment on BSA. Through competition site experiments and molecular docking, it was found that the binding site between LM and BSA was near site Ⅰ, and LM could form hydrogen bonds with Trp-213 on BSA, and there were van der Waals forces between LM and Tyr-340/451 residues.

     

/

返回文章
返回