Combining Molecular Docking and Molecular Dynamics Simulation to Discover Four Novel Umami Peptides from Tuna Skeletal Myosin with Sensory Evaluation Validation

This work aimed to identify umami peptides from tuna skeletal myosin by a novel model method of combining molecular docking and molecular dynamics simulation, to explore their umami mechanism, and to further validate the umami tastes with sensory evaluation. Four novel umami peptides (LADW, MEIDD, VAEQE, and EEAEGT) were discovered, and all of them bound to T1R1/T1R3 receptor protein via hydrogen bonds and van der Waals forces to form stable complexes, among which LADW exhibited the best affinity energy (-9.2 kcal/mol) and binding ability. Sensory evaluation and electronic tongue analyses confirmed that all peptides possessed an umami taste, and LADW exhibited the strongest umami intensity. This study may not only explore four novel umami peptides to improve the value of tuna skeletal myosin, but also provide a new method for quickly finding umami peptides.