Supramolecular self-assembly strategies of natural-based β-lactoglobulin modulating bitter perception of goat milk–derived bioactive peptides

• Published in: Journal of dairy science Vol. 107; no. 7; pp. 4174 - 4188
• Main Authors: Zhang, Rong, Jia, Wei
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.07.2024; Elsevier
• Subjects: Animals; bitter peptide; bitterness; dairy science; Gibbs free energy; goat milk; Goats; hydrogen; hydrophobicity; Lactoglobulins - chemistry; Milk - chemistry; Molecular Dynamics Simulation; peptides; Peptides - chemistry; proteomics; self-assembly; stoichiometry; Taste; UHPLC-Q-Orbitrap HRMS; β-lactoglobulin; UHPLC-Q-Orbitrap HRMS; self-assembly; bitter peptide; β-lactoglobulin
• ISSN: 0022-0302; 1525-3198; 1525-3198
• DOI: 10.3168/jds.2023-24386

The list of standard abbreviations for JDS is available at adsa.org/jds-abbreviations-24. Nonstandard abbreviations are available in the Notes. 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-LG and β-LG-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-LG in a 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 a 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 aims to provide valuable physical insights into the macroscopic self-assembly behavior between proteins and bitter peptides, and the meticulous design of highly acceptable taste characteristics in goat milk products.