David Stephen, A (2021) Validation of crystal structure of 2‐acetamidophenyl acetate: an experimental and theoretical study. JOURNAL OF BIOMOLECULAR STRUCTURE AND DYNAMICS.

[thumbnail of 36. 2 acetamidophenyl acetate.pdf] Text
36. 2 acetamidophenyl acetate.pdf
Download (3MB)

Abstract

In this present study, we have determined the crystal structure of 2-acetamidophenyl acetate (2-AAPA)
commonly used as influenza neuraminidase inhibitor, to analyze the polymorphism. Molecular docking
and molecular dynamics have been performed for the 2-AAPA-neuraminidase complex as the esterderived benzoic group shows several biological properties. The X-ray diffraction studies confirmed that
the 2-AAPA crystals are stabilized by N–H���O type of intermolecular interactions. Possible conformers
of 2-AAPA crystal structures were computationally predicted by ab initio methods and the stable crystal structure was identified. Hirshfeld surface analysis of both experimental and predicted crystal structure exhibits the intermolecular interactions associated with 2D fingerprint plots. The lowest docking
score and intermolecular interactions of 2-AAPA molecule against influenza neuraminidase confirm the
binding affinity of the 2-AAPA crystals. The quantum theory of atoms in molecules analysis of these
intermolecular interactions was implemented to understand the charge density redistribution of the
molecule in the active site of influenza neuraminidase to validate the strength of the interactions.

Item Type: Article
Uncontrolled Keywords: Acetamidophenyl acetate; neuraminidase complex; polymorphic search molecular docking; molecular dynamics simulatio
Divisions: PSG College of Arts and Science > Department of Physics
Depositing User: Mr Team Mosys
Date Deposited: 29 Jun 2022 10:40
Last Modified: 29 Jun 2022 10:40
URI: http://ir.psgcas.ac.in/id/eprint/1271

Actions (login required)

View Item
View Item
Altmetric