Chi Zhenxing, Zhao Jing, Li Weiguo, Araghi Arash, Tan Songwen
School of Marine Science and Technology, Harbin Institute of Technology, Weihai, 264209, PR China; State Key Laboratory of Urban Water Resource and Environment, Harbin Institute of Technology, Harbin 150090, PR China; Guangzhou Key Laboratory of Environmental Exposure and Health, School of Environment, Jinan University, Guangzhou 510632, PR China.
School of Marine Science and Technology, Harbin Institute of Technology, Weihai, 264209, PR China.
Chemosphere. 2017 Oct;185:29-35. doi: 10.1016/j.chemosphere.2017.07.003. Epub 2017 Jul 1.
In this work, interactions of three phthalate acid esters (PAEs), including dimethyl phthalate (DMP), diethyl phthalate (DEP) and dibutyl phthalate (DBP), with trypsin have been studied in vitro, under simulated physiological conditions using multi-spectroscopic techniques and molecular modeling. The results show that these PAEs can bind to the trypsin, forming trypsin-PAEs complexes, mainly via hydrophobic interactions, with the affinity order of DMP > DEP > DBP. Binding to the PAEs is found to result in molecular deformation of trypsin. The modeling results suggest that only DBP can bind with the amino acid residues of the catalytic triad and S1 binding pocket of trypsin, leading to potential competitive enzyme inhibition.
在本研究中，利用多光谱技术和分子模拟，在模拟生理条件下，对三种邻苯二甲酸酯（PAEs），即邻苯二甲酸二甲酯（DMP）、邻苯二甲酸二乙酯（DEP）和邻苯二甲酸二丁酯（DBP）与胰蛋白酶的相互作用进行了体外研究。结果表明，这些PAEs能与胰蛋白酶结合，形成胰蛋白酶 - PAEs复合物，主要通过疏水相互作用，亲和力顺序为DMP > DEP > DBP。发现PAEs与胰蛋白酶结合会导致其分子变形。模拟结果表明，只有DBP能与胰蛋白酶催化三联体的氨基酸残基和S1结合口袋结合，从而导致潜在的竞争性酶抑制。
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