| Title : Molecular modeling and in vitro reactivation study between the oxime BI-6 and acetylcholinesterase inhibited by different nerve agents - Giacoppo_2015_J.Biomol.Struct.Dyn_33_2048 |
| Author(s) : Giacoppo JO , Franca TCC , Kuca K , da Cunha EFF , Abagyan R , Mancini DT , Ramalho TC |
| Ref : J Biomol Struct Dyn , 33 :2048 , 2015 |
| Abstract : Nerve agents are organophosphates acting as potent inhibitors of acetylcholinesterase (AChE), the enzyme responsible for the hydrolysis of acetylcholine and, consequently, the termination of the transmission of nerve impulses. The inhibition of AChE by an organophosphate can be reversed by a nucleophilic agent able to dephosphorylate a serine residue in the active site of AChE. In this sense, the oximes are compounds capable of removing the nerve agent and reactivate the enzyme. Here, we have applied a methodology involving theoretical docking and Quantum Mechanics/Molecular Mechanics, using the softwares Molegro((R)) and Spartan((R)), to evaluate the kinetic constants of reactivation and the interactions of the oxime BI-6 with AChE inhibited by different organophosphorus compounds in comparison to in vitro data. Results confirm that this method is suitable for the prediction of kinetic and thermodynamic parameters of oximes, which may be useful in the design and selection of new and more effective oximes. |
| ESTHER : Giacoppo_2015_J.Biomol.Struct.Dyn_33_2048 |
| PubMedSearch : Giacoppo_2015_J.Biomol.Struct.Dyn_33_2048 |
| PubMedID: 25407587 |
Giacoppo JO, Franca TCC, Kuca K, da Cunha EFF, Abagyan R, Mancini DT, Ramalho TC (2015)
Molecular modeling and in vitro reactivation study between the oxime BI-6 and acetylcholinesterase inhibited by different nerve agents
J Biomol Struct Dyn
33 :2048
Giacoppo JO, Franca TCC, Kuca K, da Cunha EFF, Abagyan R, Mancini DT, Ramalho TC (2015)
J Biomol Struct Dyn
33 :2048