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Arch Biochem Biophys

Title:		Gypsy moth pheromone-binding protein-ligand interactions: pH profiles and simulations as tools for detecting polar interactions
Author(s):		Sanes JT; Plettner E;
Address:		"Department of Chemistry, Simon Fraser University, 8888 University Drive, Burnaby, BC, V5A 1S6, Canada. Department of Chemistry, Simon Fraser University, 8888 University Drive, Burnaby, BC, V5A 1S6, Canada. Electronic address: plettner@sfu.ca"
Journal Title:		Arch Biochem Biophys
Year:		2016
Volume:		20160716
Issue:
Page Number:		53 - 63
DOI:		10.1016/j.abb.2016.07.008
ISSN/ISBN:		1096-0384 (Electronic) 0003-9861 (Linking)
Abstract:		"Pheromone-binding proteins (PBPs) are believed to control diffusion of pheromones in sensory hairs of insects. The interactions of gypsy moth (Lymantria dispar) PBPs with the sex attractant pheromone, (+)-Disparlure ((7R,8S)-epoxy-2-methyloctadecane), and the enantioselectivity of recognition are not completely understood. Enantioselectivity is important for L. dispar, because (-)-disparlure cancels the attraction of (+)-disparlure, so these moths use enantiopure (+)-disparlure for communication. We performed docking simulations of the protonated homology PBP models with the enantiomers of disparlure, 5-oxadisparlure, 10-oxadisparlure, 5-thiadisparlure and 10-thiadisparlure, together with a binding assay experiment, in which the pH profiles for the PBP-ligand combinations were surveyed. The molecular simulations revealed different amino acid residues in the binding sites, movement of specific amino acid residues at certain pH values, distinct amino acid-ligand interactions (side chain donors/acceptors, H-arene bonding, backbone donors/acceptors) and differences in the conformations of each protein-ligand complex. The pKa values obtained from the binding experiment and the results from the molecular simulations served as tools for detecting polar interactions between the PBPs and ligands. The differences found between structures docked with ligand enantiomers reveal the enantioselectivity of the gypsy moth PBPs towards the pheromone and its antipode, as well as towards enantiomers of pheromone analogs with heteroatom substitutions"
Keywords:		Animals Binding Sites Carrier Proteins/*chemistry Computer Simulation Histidine/chemistry Hydrogen Bonding Hydrogen-Ion Concentration Insect Proteins/*chemistry Ligands Molecular Dynamics Simulation Moths/*metabolism Pheromones/*chemistry Protein Binding;
Notes:		"MedlineSanes, Jurgen T Plettner, Erika eng Research Support, Non-U.S. Gov't 2016/07/20 Arch Biochem Biophys. 2016 Sep 15; 606:53-63. doi: 10.1016/j.abb.2016.07.008. Epub 2016 Jul 16"