Binding Analysis of Some Classical Acetylcholinesterase Inhibitors: Insights for a Rational Design Using Free Energy Perturbation Method Calculations with QM/MM MD Simulations

Journal of Chemical Information and Modeling

Volumn 57, Issue 4, 2017, Pages 958-976

  Nascimento, Érica C M ^a,b   Oliva, Mónica ^a   Świderek, Katarzyna ^a,c   Martins, João B L ^b   Andrés, Juan ^a  

^a UNIVERSITAT JAUME I   (Spain)

^b UNIVERSITY OF BRASILIA   (Brazil)

^c LODZ UNIVERSITY OF TECHNOLOGY   (Poland)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; ELECTROSTATICS; GEOMETRY; HYDROGEN BONDS; LIGANDS; MOLECULAR DYNAMICS; MOLECULES; PERTURBATION TECHNIQUES; POSITIVE IONS; QUANTUM THEORY; VAN DER WAALS FORCES;

ACETYLCHOLINESTERASE; ACETYLCHOLINESTERASE INHIBITORS; FREE ENERGY PERTURBATION; FREE-ENERGY PERTURBATION METHODS; INTERACTION ENERGIES; MOLECULAR DYNAMICS SIMULATIONS; QM/MM MD SIMULATIONS; VAN DER WAALS INTERACTIONS;

FREE ENERGY;

ACETYLCHOLINESTERASE; CHOLINESTERASE INHIBITOR; PROTEIN BINDING;

CHEMISTRY; DRUG DESIGN; HYDROGEN BOND; METABOLISM; MOLECULAR DYNAMICS; QUANTUM THEORY; THERMODYNAMICS;

ACETYLCHOLINESTERASE; CHOLINESTERASE INHIBITORS; DRUG DESIGN; HYDROGEN BONDING; MOLECULAR DYNAMICS SIMULATION; PROTEIN BINDING; QUANTUM THEORY; THERMODYNAMICS;

EID: 85018590592     PISSN: 15499596     EISSN: 1549960X     Source Type: Journal    
DOI: 10.1021/acs.jcim.7b00037     Document Type: Article

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