Identification, Molecular Docking Mechanism and Cellular Activity of Selenium-Enriched ACE Inhibitory Peptides from Oysters.

ABSTRACT: Selenium-enriched oyster proteins were hydrolyzed using trypsin to obtain peptides with angiotensin-I-converting enzyme (ACE) inhibitory activity. The hydrolysate was purified by ultrafiltration and two-step reversed-phase high-performance liquid chromatography (RP-HPLC), yielding the most active fraction M4-2 (selenium content: 37.00 ± 0.56 mg/kg; IC₅₀: 0.774 mg/mL, significantly lower than the IC₅₀ of the crude hydrolysate, 2.801 mg/mL). This fraction was further analyzed by LC-MS/MS and molecular docking, leading to the identification of 91 selenium-containing peptide sequences. Two novel peptides, SeMFRTSSK and QASeMNEATGGK, showing strong binding affinities (-9.8 and -9.0 kcal/mol, respectively), were selected. Molecular docking revealed that SeMFRTSSK bound to k

SUBMITTER: Yue Z 

PROVIDER: S-EPMC12735907 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature