J Agric Food Chem. 2015 Jan 14;63(1):75-84. doi: 10.1021/jf5046359.
Dimethyl phthalate (DMP) is widely used as a plasticizer in industrial processes and has been reported to possess potential toxicity to the human body. In this study, the interaction between DMP and trypsin in vitro was investigated. The results of fluorescence, UV–vis, circular dichroism, and Fourier transform infrared spectra along with cyclic voltammetric measurements indicated that the remarkable fluorescence quenching and conformational changes of trypsin resulted from the formation of a DMP–trypsin complex, which was driven mainly by hydrophobic interactions. The molecular docking and trypsin activity assay showed that DMP primarily interacted with the catalytic triad of trypsin and led to the inhibition of trypsin activity. The dimensions of the individual trypsin molecules were found to become larger after binding with DMP by atomic force microscopy imaging. This study offers a comprehensive picture of DMP–trypsin interaction, which is expected to provide insights into the toxicological effect of DMP.
邻苯二甲酸二甲酯(DMP)广泛用作工业过程中的增塑剂,据报道对人体具有潜在毒性。在这项研究中,研究了 DMP 与胰蛋白酶在体外的相互作用。荧光、紫外-可见、圆二色性和傅里叶变换红外光谱以及循环伏安测量的结果表明,胰蛋白酶的显著荧光猝灭和构象变化是由于形成了 DMP-胰蛋白酶复合物所致,这主要是由疏水相互作用驱动的。分子对接和胰蛋白酶活性测定表明,DMP 主要与胰蛋白酶的催化三联体相互作用,导致胰蛋白酶活性的抑制。原子力显微镜成像表明,DMP 与单个胰蛋白酶分子结合后,其尺寸变大。这项研究提供了 DMP-胰蛋白酶相互作用的全面描述,有望深入了解 DMP 的毒理学效应。