Abstract
Complete self-assembly and reassembly behavior of bitter peptide-protein necessitates multilevel theories that encompass phenomena ranging from the self-assembly of recombinant complex to atomic trajectories. An extension to the level of mechanism method was put forth, involves limited enzymatic digestion and bottom-up proteomics to dissect inherent heterogeneity within β-lactoglobulin and β-lactoglobulin-PPGLPDKY complex and uncover conformational and dynamic alterations occurring in specific local regions of the model protein. Bitter peptide PPGLPDKY spontaneously bound to IIAEKTK, IDALNENK, and YLLFCMENSAEPEQSLACQCLVR regions of β-lactoglobulin in 1:1 stoichiometric ratio to mask bitterness perception. Molecular dynamic simulation and free energy calculation provided time-varying atomic trajectories of the recombinant complex, and found that peptide was stabilized in the upper region of the hydrophobic cavity with the binding free energy of -30.56 kJ mol-1 through 4 hydrogen bonds (Glu74, Glu55, Lys69, and Ser116) and hydrophobic interactions (Asn88, Asn90 and Glu112). Current research endeavors to provide valuable physical insights into the macroscopic self-assembly behavior between protein and bitter peptide, and the meticulous design of highly acceptable taste characteristics in goat milk products.
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