| 韩永光,安 娜,闫 蕊,李晓飞.盐酸比哌立登与人血清蛋白的相互作用研究[J].,2018,(18):3435-3439 |
| 盐酸比哌立登与人血清蛋白的相互作用研究 |
| Study on the Interaction of Biperiden Hydrochloride with Human Serum Albumin |
| 投稿时间：2018-03-17 修订日期：2018-04-13 |
| DOI：10.13241/j.cnki.pmb.2018.18.007 |
| 中文关键词: 盐酸比哌立登 人血清蛋白 荧光光谱 傅里叶变换红外光谱 分子模拟 |
| 英文关键词: Biperiden Hydrochloride Human serum albumin Fluorescence spectrometry Fourier Transform Infrared Spectroscopy Molecular docking |
| 基金项目:河南省高等学校重点科研计划项目（15B350002） |
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| 中文摘要: |
| 摘要 目的：研究盐酸比哌立登（BH）与人血清蛋白（HSA）的相互作用,为阐明其在体外的代谢过程、作用机理提供理论依据。方法：本研究采用紫外 -可见分光光度法、荧光光谱法、傅里叶变换红外光谱（FTIR）法及分子对接模拟等方法，在不同温度下，测定BH与 HAS的紫外吸收光谱变化、结合常数、结合位点，蛋白质二级结构变化和分子模拟对接情况。结果：在 25℃时，BH与 HSA的结合常数 KA为 2.71× 103L/mol，结合位点数目是 0.86；在 37℃时，结合常数 KA为 1.58× 103L/mol，结合位点数目为 0.82。BH使得 HSA的荧光波长向短波长方向蓝移；BH可导致 HSA的琢-螺旋向无规卷曲的转变。结论：BH与 HAS通过氢键和范德华力相互作用，导致 HSA酪氨酸残基周围内环境被破坏，环境极性减弱，疏水性增加，同时还会导致 HSA荧光静态猝灭。 |
| 英文摘要: |
| ABSTRACT Objective: To elucidate the metabolic process of BH in vitro and provide theoretical basis for its mechanism of action, the interaction between Biperiden Hydrochloride(BH) with human serum albumin (HSA) was investigated. UV absorption spectra, binding constants, binding sites, protein secondary structure changes and molecular docking of BH and HAS were measured under different temperatures. Methods:The interaction between BH and HSA was studied by UV-visible spectrophotometry, fluorescence spectrometry, Fourier transform infrared spectroscopy (FTIR) method and molecular connection simulation. Results:The number of bingding sites was approximately 0.86 and the bingding constant Ka was 2.71× 103 L/mol at 298 K, while the number of bingding sites was approximately 0.82 and the bingding constant Ka was 1.58× 103 L/mol at 310K. The main fluorescence peaks of HSA shifted markedly to shorter wavelenth on account of BH and the α-helix of HSA changs to the random crimp on account of BH. Conclusion:The thermodynamic parameters show that the binding foroce between BH and HSA is mainly the hydrogen bond and van der Waals force. BH could lead to HSA Static quenching fluorescence, disturb the protein's structure around tyrosine residues and increase the protein hydrophobic. BH also lead to HSA static quenching fluorescence. |
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