Study on the different replacing groups of trans-paroxol for enzymatic resolution using molecular simulations

Chuan Zhang, Yigang Jia, Chao Xu, He Huang, Yi Hu

Research output: Chapter in Book/Report/Conference proceedingConference contributionpeer-review

Abstract

Trans-paroxol is an important key intermediate for paroxetine synthesis. Four different replacing groups of trans-paroxol on the kinetic resolution were studied to illuminate the mechanism of enzymatic catalysis using molecular simulations. Hydrogen bonds, hydrophobic interactions and the protein structure were analysed for enzyme-substrate complex. Results indicated that the formation of hydrogen bond, hydrophobic interactions and the distribution of substrate conformation in active site were the major forces which resulted in the diversity of enzymatic resolution. Electrostatic interactions and the stability of complex also played an important role in this reaction. This study will be quite useful for understanding the mechanism of enzymatic resolution and guiding to design the appropriate substrate for paroxetine synthesis.

Original languageEnglish
Title of host publicationAdvances in Applied Biotechnology - Proceedings of the 3rd International Conference on Applied Biotechnology, ICAB 2016
EditorsHao Liu, Arthur Ram, Cunjiang Song
PublisherSpringer Verlag
Pages365-374
Number of pages10
ISBN (Print)9789811048005
DOIs
StatePublished - 2018
Externally publishedYes
Event3rd International Conference on Applied Biotechnology, ICAB 2016 - Tianjin, China
Duration: 25 Nov 201627 Nov 2016

Publication series

NameLecture Notes in Electrical Engineering
Volume444
ISSN (Print)1876-1100
ISSN (Electronic)1876-1119

Conference

Conference3rd International Conference on Applied Biotechnology, ICAB 2016
Country/TerritoryChina
CityTianjin
Period25/11/1627/11/16

Keywords

  • Enzymatic resolution
  • Molecular docking
  • Molecular dynamics simulations
  • Paroxetine
  • Trans-Paroxol

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