Validation of crystal structure of 2?acetamidophenyl acetate: an experimental and theoretical study
[ X ]
Tarih
2022
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Taylor and Francis Ltd.
Erişim Hakkı
info:eu-repo/semantics/openAccess
Özet
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 ester-derived 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. Communicated by Ramaswamy H. Sarma. © 2021 Informa UK Limited, trading as Taylor & Francis Group.
Açıklama
Anahtar Kelimeler
Acetamidophenyl acetate; molecular docking; molecular dynamics simulation; neuraminidase complex; polymorphic search
Kaynak
Journal of Biomolecular Structure and Dynamics
WoS Q Değeri
Scopus Q Değeri
Q1
Cilt
40
Sayı
23
