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    基于分子光谱法、热动力学分析法和分子对接技术的丁香酸甲酯和人血清白蛋白相互作用机制的研究

    Study on Interaction Mechanism Between Methyl Syringate and Human Serum Albumin Based on Molecular Spectrometry, Thermodynamic Analysis and Molecular Docking Technology

    • 摘要: 丁香酸甲酯作为特定蜂蜜的特征性标志物,在进入人体后可与人血清白蛋白(HSA)结合并通过血液循环实现全身运输,但目前对二者的相互作用机制尚缺乏系统研究。为此,采用题示方法系统考察了丁香酸甲酯与HSA相互作用的荧光猝灭特性、分子间作用力类型、能量转移机制及特异性结合模式。采用荧光光谱法、紫外-可见吸收光谱法和热动力学分析法分析,结果显示,丁香酸甲酯与HSA以5.82 nm的结合距离通过氢键、范德华力和疏水相互作用力相结合,引发非辐射能量转移,导致HSA发生动态荧光猝灭并伴随最大发射波长红移;同步荧光光谱法分析结果表明,随着丁香酸甲酯浓度的增大,色氨酸(Trp)残基和酪氨酸(Tyr)残基的特征荧光强度逐渐降低,提示HSA微环境疏水性下降,肽链伸展程度增加,蛋白质构象发生改变;分子对接模型显示,丁香酸甲酯可进入HSA结合口袋,与氨基酸残基,如Tyr残基Tyr-138和组氨酸(His)残基His-146等形成氢键,这一特异性结合模式可能是产生上述现象的结构基础。研究阐明了丁香酸甲酯与HSA的动态相互作用机制,可为深入理解蜂蜜特征成分的体内运输过程及其潜在生理功能提供重要的理论基础。

       

      Abstract: Methyl syringate, as a characteristic marker of specific honey varieties, can bind to human serum albumin (HSA) after entering the human body and achieve systemic transport through blood circulation, but their interaction mechanism still lacks systematic research. To address this, the methods mentioned by the title were employed to systematically investigate the fluorescence quenching characteristics, types of intermolecular forces, energy transfer mechanisms, and specific binding patterns between methyl syringate and HSA. As found by the results of fluorescence spectrometry, ultraviolet-visible absorption spectrometry and thermodynamic analysis, methyl syringate was bound to HSA with interaction distance of 5.82 nm through hydrogen bonds, van der Waals forces, and hydrophobic interaction forces, triggering non-radiative energy transfer that led to dynamic fluorescence quenching of HSA accompanied by a red shift in the maximum emission wavelength. As shown by the results of synchronous fluorescence spectrometry analysis, as the concentration of methyl syringate increased, the characteristic fluorescence intensities of tryptophan (Trp) residue and tyrosine (Tyr) residue gradually decreased, indicating decreased hydrophobicity decrease in the HSA microenvironment, the increase of peptide chain extension, and conformational changes in the protein. As demonstrated by the molecular docking model, methyl syringate could enter the binding pocket of HSA and form hydrogen bonds with amino acid residues, such as Tyr residue Tyr-138 and histidine (His) residue His-146, and this specific binding pattern might serve as the structural basis for the aforementioned phenomena. The dynamic interaction mechanism between methyl syringate and HSA was elucidated in this study, which could provide an important theoretical foundation for deeper understanding of the in vivo transport processes and potential physiological functions of honey´s characteristic components.

       

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