摘要
天然产物芦丁(Rutin)可以抑制弹性蛋白酶的活性,采用多光谱法与分子对接技术研究芦丁与弹性蛋白酶(PPE)的相互作用。研究结果表明,Rutin对PPE存在荧光猝灭效应,且为静态猝灭。Rutin与PPE能形成1∶1复合物,在298 K下其结合常数为4.90×10^(4) L/mol,主要结合力为氢键和范德华力。根据Forster′s非辐射能量转移理论,计算得到Rutin与PPE的结合距离r为4.55 nm。紫外光谱与同步荧光光谱结果表明,Rutin可使PPE周围微环境发生改变,极性增加、亲水性增加和疏水性减弱。傅里叶变换红外光谱与圆二色光谱分析表明,Rutin使PPE的α-螺旋、β-折叠含量降低,酶结构变得松散,改变了PPE的二级结构。分子对接模拟表明,Rutin与PPE距离在0.4 nm之内的氨基酸残基共有11个,共形成5条氢键,同时还有强大的范德华力与π-阳离子相互作用,多种作用力使Rutin与PPE形成稳定的复合物,抑制了弹性蛋白酶的活性。
The natural product Rutin can inhibit the activity of elastase.The interaction between Rutin and elastase(PPE)was studied by multispectral method and molecular docking techniques.The results showed that Rutin quenched the fluorescence of elastase and it was static quenching.Rutin and elastase could form a 1∶1 complex with a binding constant of 4.90×10^(4) L/mol at 298 K,the main binding force was hydrogen bonds and van der Waals force between Rutin and elastase.The binding distance between Rutin and elastase was calculated to be 4.55 nm according to Forster′s non-radiative energy transfer theory.The results of ultraviolet spectrum(UV)and synchronous fluorescence spectrum(SFS)showed that Rutin could change the microenvironment around PPE,increasing polarity,increasing hydrophilicity and decreasing hydrophobicity.Fourier transform infrared(FT-IR)and circular dichroism spectra(CD)showed that Rutin reduced the content ofα-helix andβ-fold of PPE,made the elastase structure more loose,and changed the secondary structure of PPE.The molecular docking simulation showed that there were 11 amino acid residues within 0.4 nm distance between Rutin and PPE,and five hydrogen bonds were formed.At the same time,there were strong van der Waals forces interacting withπ-cation,thus multiple forces exist between Rutin and elastase system to form a stable compound,which inhibitedthe activity of elastase.
作者
姚红柳
付金凤
尹广婷
周雪健
苏丽红
YAO Hong-liu;FU Jin-feng;YIN Guang-ting;ZHOU Xue-jian;SU Li-hong(College of Chemistry,Changchun Normal University,Changchun 130032,China)
出处
《化学试剂》
CAS
北大核心
2022年第1期46-51,共6页
Chemical Reagents
基金
吉林省科技厅项目(20140101043JC)
吉林省教育厅项目(吉教科合字[2013]第251号)
长春师范大学自然科学基金资助项目(长师大自科合字[2018]第016号)。