Fuente: PubMed "royal jelly" Food Res Int. 2026 Apr 1;229:118476. doi: 10.1016/j.foodres.2026.118476. Epub 2026 Jan 22.ABSTRACTRoyal jelly proteins (RJPs) are rich sources of bioactive peptides with health-promoting functions. This study aimed to identify and characterize angiotensin-I-converting enzyme (ACE) inhibitory peptides derived from the gastrointestinal digest of RJPs using an integrated peptidomics and bioinformatics strategy. A total of 1983 peptides were identified by LC-MS/MS, of which 237 exhibited high predicted bioactivity (PeptideRanker score ≥ 0.8). After in silico screening, 49 soluble bioactive peptides were selected, showing favorable molecular weights, charge properties, and oral bioavailability. Bioactivity profiling suggested multiple functions, with ACE inhibition emerging as the most dominant. Molecular docking confirmed strong ACE binding affinities for all of the selected peptides (-6.9 to -10.9 kcal/mol), surpassing the positive control captopril (-5.6 kcal/mol). Experimental validation showed FRYR and FFRNR possessed strong ACE inhibitory activity, with IC50 values of 608 μmol/L and 684 μmol/L, respectively, lower than many reported food-derived peptides. Kinetic analysis revealed FRYR exhibited mixed-type inhibition, while FFRNR acted competitively. Docking revealed FRYR uniquely coordinated with the Zn2+ catalytic center, explaining its superior potency. Collectively, these results highlight the digest of RJPs as promising sources of natural ACE inhibitors and provide a systematic strategy for bioactive peptide discovery and functional validation.PMID:41763798 | DOI:10.1016/j.foodres.2026.118476