Identification of salty peptides from enzymolysis extract of oyster by peptidomics and virtual screening.

[Display omitted] • A peptidomics and virtual screening approach was used to screen salty peptides. • Four salty peptides were identified from the enzymatic hydrolysate of oyster. • All the salty peptides were capable of binding to the cavity of TMC4. • Thr581, Arg312, Arg294, Ala298 and Glu319 of TMC4 were the domain binding sites. Salty peptide as an important sodium substitute, which could reduce the risk of cardiovascular disease caused by excessive sodium intake. In this study, novel salty peptides were prepared and identified from enzymolysis extract of oysters by peptitomic identification, virtual screening and solid phase synthesis. Additionally, molecular simulation was used to study the taste mechanism of salty peptides. 316 peptides were identified in the enzymatic hydrolysates of oysters. 6 peptides, selected through virtual screening, were synthesized using solid-phase synthesis, and EK, LFE, LEY and DR were confirmed to possess a pleasing salty taste through electronic tongue evaluation. Molecular docking results indicated that these 4 peptides could enter the binding pocket within the transmembrane channel-like 4 (TMC4) cavity, wherein salt bridges, hydrogen bonds and attractive charges were the main binding forces. This study provides a rapid screening method for salty peptides in sea food products but possibly applied for other sources. [ABSTRACT FROM AUTHOR]

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