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Int. J. Mol. Sci. 2015, 16(3), 6217-6234; doi:10.3390/ijms16036217

Molecular Dynamics Simulations of Acylpeptide Hydrolase Bound to Chlorpyrifosmethyl Oxon and Dichlorvos

Key Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, College of Life Science, Jilin University, Changchun 130023, China
Second Bethune Hospital of Jilin University, Changchun 130041, China
State Key Laboratory of Theoretical and Computational Chemistry, Institute of Theoretical Chemistry, Jilin University, Changchun 130023, China
These authors contributed equally to this work.
Author to whom correspondence should be addressed.
Academic Editor: Tatyana Karabencheva-Christova
Received: 23 December 2014 / Revised: 3 February 2015 / Accepted: 4 March 2015 / Published: 18 March 2015
(This article belongs to the Collection Proteins and Protein-Ligand Interactions)
View Full-Text   |   Download PDF [3421 KB, uploaded 18 March 2015]   |  


Acylpeptide hydrolases (APHs) catalyze the removal of N-acylated amino acids from blocked peptides. Like other prolyloligopeptidase (POP) family members, APHs are believed to be important targets for drug design. To date, the binding pose of organophosphorus (OP) compounds of APH, as well as the different OP compounds binding and inducing conformational changes in two domains, namely, α/β hydrolase and β-propeller, remain poorly understood. We report a computational study of APH bound to chlorpyrifosmethyl oxon and dichlorvos. In our docking study, Val471 and Gly368 are important residues for chlorpyrifosmethyl oxon and dichlorvos binding. Molecular dynamics simulations were also performed to explore the conformational changes between the chlorpyrifosmethyl oxon and dichlorvos bound to APH, which indicated that the structural feature of chlorpyrifosmethyl oxon binding in APH permitted partial opening of the β-propeller fold and allowed the chlorpyrifosmethyl oxon to easily enter the catalytic site. These results may facilitate the design of APH-targeting drugs with improved efficacy. View Full-Text
Keywords: acylpeptide hydrolase; organophosphorus compound; docking study; molecular dynamics simulation acylpeptide hydrolase; organophosphorus compound; docking study; molecular dynamics simulation

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Jin, H.; Zhou, Z.; Wang, D.; Guan, S.; Han, W. Molecular Dynamics Simulations of Acylpeptide Hydrolase Bound to Chlorpyrifosmethyl Oxon and Dichlorvos. Int. J. Mol. Sci. 2015, 16, 6217-6234.

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