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In vitro assessment of phthalate acid esters-trypsin complex formation.
Chemosphere. 2017 Oct; 185:29-35.C

Abstract

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.

Authors+Show Affiliations

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. Electronic address: zhenxingchi@gmail.com.School of Marine Science and Technology, Harbin Institute of Technology, Weihai, 264209, PR China.School of Marine Science and Technology, Harbin Institute of Technology, Weihai, 264209, PR China.School of Chemical and Biomolecular Engineering, The University of Sydney, Sydney 2006, Australia.School of Marine Science and Technology, Harbin Institute of Technology, Weihai, 264209, PR China.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

28683334

Citation

Chi, Zhenxing, et al. "In Vitro Assessment of Phthalate Acid Esters-trypsin Complex Formation." Chemosphere, vol. 185, 2017, pp. 29-35.
Chi Z, Zhao J, Li W, et al. In vitro assessment of phthalate acid esters-trypsin complex formation. Chemosphere. 2017;185:29-35.
Chi, Z., Zhao, J., Li, W., Araghi, A., & Tan, S. (2017). In vitro assessment of phthalate acid esters-trypsin complex formation. Chemosphere, 185, 29-35. https://doi.org/10.1016/j.chemosphere.2017.07.003
Chi Z, et al. In Vitro Assessment of Phthalate Acid Esters-trypsin Complex Formation. Chemosphere. 2017;185:29-35. PubMed PMID: 28683334.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - In vitro assessment of phthalate acid esters-trypsin complex formation. AU - Chi,Zhenxing, AU - Zhao,Jing, AU - Li,Weiguo, AU - Araghi,Arash, AU - Tan,Songwen, Y1 - 2017/07/01/ PY - 2017/03/11/received PY - 2017/06/08/revised PY - 2017/07/01/accepted PY - 2017/7/7/pubmed PY - 2017/11/3/medline PY - 2017/7/7/entrez KW - Molecular modeling KW - Multi-spectroscopic techniques KW - Phthalate acid esters KW - Toxicity KW - Trypsin SP - 29 EP - 35 JF - Chemosphere JO - Chemosphere VL - 185 N2 - 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. SN - 1879-1298 UR - https://www.unboundmedicine.com/medline/citation/28683334/In_vitro_assessment_of_phthalate_acid_esters_trypsin_complex_formation_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0045-6535(17)31046-9 DB - PRIME DP - Unbound Medicine ER -