Paper Info
Title
Molecular recognition of thiaclopride by Aplysia californica AChBP: new insights from a computational investigation.
Abstract
The binding of thiaclopride (THI), a neonicotinoid insecticide, with Aplysia californica acetylcholine binding protein (Ac-AChBP), the surrogate of the extracellular domain of insects nicotinic acetylcholine receptors, has been studied with a QM/QM' hybrid methodology using the ONIOM approach (M06-2X/6-311G(d):PM6). The contributions of Ac-AChBP key residues for THI binding are accurately quantified from a structural and energetic point of view. The importance of water mediated hydrogen-bond (H-bond) interactions involving two water molecules and Tyr55 and Ser189 residues in the vicinity of the THI nitrile group, is specially highlighted. A larger stabilization energy is obtained with the THI-Ac-AChBP complex compared to imidacloprid (IMI), the forerunner of neonicotinoid insecticides. Pairwise interaction energy calculations rationalize this result with, in particular, a significantly more important contribution of the pivotal aromatic residues Trp147 and Tyr188 with THI through CH···π/CH···O and π-π stacking interactions, respectively. These trends are confirmed through a complementary non-covalent interaction (NCI) analysis of selected THI-Ac-AChBP amino acid pairs.
Year
DOI
Venue
2015
10.1007/s10822-015-9884-x
Journal of Computer-Aided Molecular Design
Keywords
Field
DocType
Thiacloprid,AChBP,ONIOM calculations,Neonicotinoids
Binding site,Molecular recognition,Computational chemistry,Molecular Docking Simulation,Chemistry,Acetylcholine binding,ONIOM,Interaction energy,Stereochemistry,Hydrogen bond,Stacking
Journal
Volume
Issue
ISSN
29
12
1573-4951
Citations 
PageRank 
References 
0
0.34
4
Authors
9
Name
Order
Citations
PageRank
Zakaria Alamiddine100.68
Balaji Selvam200.34
Jose P. Ceron Carrasco301.01
Monique Mathé-Allainmat400.68
Jacques Lebreton500.68
Steeve H Thany600.68
Adèle D. Laurent701.35
Jérôme Graton821.05
Jean-Yves Le Questel921.39