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Interaction mechanism of a natural medicine product helicid with a typical digestive enzyme trypsin
Spectroscopy Letters ( IF 1.7 ) Pub Date : 2020-12-09 , DOI: 10.1080/00387010.2020.1855451
Min Tang 1 , Limin Wang 1 , Guangyao Zhao 1 , Qingguo Han 1 , Xu Xu 1 , Zheling Zeng 2 , Ming Ying 1 , Zhendan He 3 , Zhangli Hu 1 , Hong Xu 1
Affiliation  

Abstract

The interaction mechanism of a kind of natural drug helicid with typical digestive enzyme trypsin was investigated using multi-spectroscopic techniques and molecular modeling method. The fluorescence quenching experiments showed that helicid quenched trypsin fluorescence via a combined quenching mechanism of both dynamic and static quenching processes because of the formation of the helicid–trypsin complex. Thermodynamic analyses suggested that the binding of helicid to trypsin was entropy-driven, and that hydrophobic interactions are the main force to stabilize the complex. Förster energy transfer theory applied demonstrated that energy transfer occurred within the complex. Ultraviolet-visible spectroscopy, synchronous fluorescence spectroscopy, three-dimension fluorescence spectroscopy together with circular dichroism spectroscopy indicated that the conformation of trypsin changed induced by helicid with the loosening of the polypeptide backbone of trypsin and its partial β-sheet and random coil structures being transformed into an α-helix structure and that helicid was closer to tryptophan residues than to tyrosine residues within the complex. Molecular simulation results explained the above experimental results very well and further implied that besides hydrophobic interactions, hydrogen bonds also helped stabilize the helicid–trypsin complex. This study is helpful to the understanding of the biochemical process of helicid in the human body and could provide useful information for the studies on the structure–bioactivity relationship of natural compounds, as well as the design and optimization of the drugs for the treatments of trypsin overactivity-related diseases.



中文翻译:

天然药物螺旋体与典型的消化酶胰蛋白酶的相互作用机理

摘要

利用多光谱技术和分子模拟方法研究了一种天然药物螺旋体与典型的消化酶胰蛋白酶的相互作用机理。荧光猝灭实验表明,由于螺旋-胰蛋白酶复合物的形成,螺旋体通过动态和静态猝灭过程的组合猝灭机制对胰蛋白酶进行了荧光猝灭。热力学分析表明,螺旋体与胰蛋白酶的结合是由熵驱动的,并且疏水相互作用是稳定该复合物的主要力量。应用的Förster能量转移理论表明,能量转移发生在复合体内。紫外可见光谱,同步荧光光谱,三维荧光光谱和圆二色光谱表明,由于胰蛋白酶的多肽主链的松弛以及部分β-折叠和无规卷曲结构被转变为α-螺旋结构而导致的螺旋结构改变了胰蛋白酶的构象更接近色氨酸残基而不是复合物中的酪氨酸残基。分子模拟结果很好地解释了上述实验结果,并进一步暗示,除了疏水相互作用外,氢键还有助于稳定螺旋-胰蛋白酶复合物。这项研究有助于理解螺旋藻在人体内的生化过程,并且可以为研究天然化合物的结构-生物活性关系提供有用的信息,

更新日期:2020-12-09
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