Probing the reactivation process of sarin-inhibited acetylcholinesterase with α-nucleophiles: Hydroxylamine anion is predicted to be a better antidote with DFT calculations

Journal of Molecular Graphics and Modelling

Volumn 29, Issue 8, 2011, Pages 1039-1046

  Khan, Md Abdul Shafeeuulla ^a   Lo, Rabindranath ^a   Bandyopadhyay, Tusar ^b   Ganguly, Bishwajit ^a  

^a CSIR CENTRAL SALT AND MARINE CHEMICALS RESEARCH INSTITUTE   (India)

^b BHABHA ATOMIC RESEARCH CENTRE   (India)

Author keywords

Alpha nucleophiles; Density functional calculations; Hydroxylamine anion; OP inihited AChE; Reactivation

Indexed keywords

ALPHA-NUCLEOPHILES; DENSITY FUNCTIONAL CALCULATIONS; HYDROXYLAMINE ANION; OP-INIHITED ACHE; REACTIVATION;

AMINES; AMINO ACIDS; ENZYME INHIBITION; HYDROGEN; HYDROGEN BONDS; NUCLEOPHILES; REACTION KINETICS;

IONS;

ACETYLCHOLINESTERASE; ALPHA NUCLEOPHILE; ANION; CARBONYL DERIVATIVE; FORMOXIMATE ANION; GLUTAMIC ACID; GLYCINE; HYDROXYLAMINE; NUCLEOPHILE; SARIN; SARIN INHIBITED ACETYLCHOLINESTERASE; SERINE; UNCLASSIFIED DRUG;

ARTICLE; DENSITY FUNCTIONAL THEORY; ENZYME INACTIVATION; ENZYME REACTIVATION; HYDROGEN BOND; PRIORITY JOURNAL;

ACETYLCHOLINESTERASE; ANIONS; CHOLINESTERASE INHIBITORS; CHOLINESTERASE REACTIVATORS; COMPUTER SIMULATION; ENZYME ACTIVATION; HUMANS; HYDROGEN BONDING; HYDROXYLAMINE; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; SARIN; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 79957902945     PISSN: 10933263     EISSN: 18734243     Source Type: Journal    
DOI: 10.1016/j.jmgm.2011.04.009     Document Type: Article

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