Low-Energy Conformations of Delicious Peptide, a Food Flavor. Study by Quenched Molecular Dynamics and NMR

NMR and quenched molecular dynamics investigations of Delicious Peptide are reported. Four families of structures are derived from the molecular dynamics simulation, which can be considered as cyclic, due to hydrogen bonding from the first residue to the end of the chain, or S-shaped. The S-shaped family contains the lowest energy structures, which is consistent with the NMR results obtained. The families of structures display interactions between the acidic and basic parts of the molecule, which is consistent with the currently accepted theory for the flavor-inducing properties of this peptide. Keywords: Flavor peptides; NMR; quenched molecular dynamics