Pnictogen bond-driven control of the molecular interaction between organophosphorus and acetylcholinesterase enzyme

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62690094%3A18450%2F24%3A50021353" target="_blank" >RIV/62690094:18450/24:50021353 - isvavai.cz</a>

Výsledek na webu

<a href="https://onlinelibrary.wiley.com/doi/10.1002/jcc.27328" target="_blank" >https://onlinelibrary.wiley.com/doi/10.1002/jcc.27328</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/jcc.27328" target="_blank" >10.1002/jcc.27328</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Pnictogen bond-driven control of the molecular interaction between organophosphorus and acetylcholinesterase enzyme

Popis výsledku v původním jazyce

This study addresses a comprehensive assessment of the interaction between chemical warfare agents (CWA) and acetylcholinesterase (AChE) systems, focus on the intriguing pnictogen-bond interaction (PnB). Utilizing the crystallographic data from the Protein Data Bank pertaining to the AChE-CWA complex involving Sarin (GB), Cyclosarin (GF), 2-[fluoro(methyl)phosphoryl]oxy-1,1-dimethylcyclopentane (GP) and venomous agent X (VX) agents, the CWA is systematically displaced by increments of 0.1 Å along the P-O bond axis, extending its distance by 4 Å from the original position. The AIM analysis was carried out and consistently revealed the presence of a significant interaction along the P-O bond. Investigating the intrinsic nature of the PnB, the NBO and the EDA analysis unearthed the contribution of orbital factors to the overall energy of the system. Strikingly, this observation challenges the conventional σ-hole explanation commonly associated with such interactions. This finding adds a layer of complexity to understanding of PnB, encouraging further exploration into the underlying mechanisms governing these intriguing chemical phenomena. © 2024 The Authors. Journal of Computational Chemistry published by Wiley Periodicals LLC.

Název v anglickém jazyce

Pnictogen bond-driven control of the molecular interaction between organophosphorus and acetylcholinesterase enzyme

Popis výsledku anglicky

This study addresses a comprehensive assessment of the interaction between chemical warfare agents (CWA) and acetylcholinesterase (AChE) systems, focus on the intriguing pnictogen-bond interaction (PnB). Utilizing the crystallographic data from the Protein Data Bank pertaining to the AChE-CWA complex involving Sarin (GB), Cyclosarin (GF), 2-[fluoro(methyl)phosphoryl]oxy-1,1-dimethylcyclopentane (GP) and venomous agent X (VX) agents, the CWA is systematically displaced by increments of 0.1 Å along the P-O bond axis, extending its distance by 4 Å from the original position. The AIM analysis was carried out and consistently revealed the presence of a significant interaction along the P-O bond. Investigating the intrinsic nature of the PnB, the NBO and the EDA analysis unearthed the contribution of orbital factors to the overall energy of the system. Strikingly, this observation challenges the conventional σ-hole explanation commonly associated with such interactions. This finding adds a layer of complexity to understanding of PnB, encouraging further exploration into the underlying mechanisms governing these intriguing chemical phenomena. © 2024 The Authors. Journal of Computational Chemistry published by Wiley Periodicals LLC.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

30108 - Toxicology

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2024

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Computational Chemistry

ISSN

0192-8651

e-ISSN

1096-987X

Svazek periodika

45

Číslo periodika v rámci svazku

15

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

13

Strana od-do

1303-1315

Kód UT WoS článku

001163168500001

EID výsledku v databázi Scopus

2-s2.0-85185658417