Characterization of Umami Dry-Cured Ham-Derived Dipeptide Interaction with Metabotropic Glutamate Receptor (mGluR) by Molecular Docking Simulation

Abstract

Dry-cured ham-derived dipeptides, generated along a dry-curing process, are of high importance since they play a role in flavor development of dry-cured ham. The objective of this study was to analyze the residues of the less-studied metabotropic glutamate receptor 1 (mGluR1) implicated in the recognition of umami dry-cured ham dipeptides by molecular docking simulation using the AutoDock Suite tool. AH, DA, DG, EE, ES, EV, and VG (and glutamate) were found to attach the enzyme with inhibition constants ranging from 12.32 µM (AH) to 875.75 µM (ES) in the case if Rattus norvegicus mGluR1 and 17.44 µM (VG) to 294.68 µM (DG) in the case of Homo sapiens, in the open–open conformations. Main interactions were done with key receptor residues Tyr74, Ser186, Glu292, and Lys409; and Ser165, Ser186, and Asp318, respectively, for the two receptors in the open–open conformations. However, more residues may be involved in the complex stabilization. Specifically, AH, EE and ES relatively established a higher number of H-bonds, but AH, EV, and VG presented relatively lower Ki values in all cases. The results obtained here could provide information about structure and taste relationships and constitute a theoretical reference for the interactions of novel umami food-derived peptides.