Antioxidant, Hypotensive, and Antidiabetic Breakthroughs: Bromelain Hydrolysis Unlocks Quinoa’s Peptide Potential - In Silico and In Vitro Approach

This study integrates bioinformatics and experimental approaches to characterize bioactive peptides derived from quinoa 11S-globulin (Chenopodium quinoa Willd) hydrolyzedin silico by stem bromelain (EC3.4.22.32). A total of 109 peptides were generated, of which 14 sequences with more than five amino acids were selected based on molecular docking and dynamics simulations against key metabolic targets (ACE-I, DPP-IV, α-glucosidase, and lipoxygenase). NIYQIS and QDQHQKIR demonstrated the highest binding affinities and hydrogen-bonding interactions, with ADMET predictions confirming their non-toxic and bioavailable profiles. In vitro, NIYQIS showed the strongest inhibitory activity against ACE-I (53%), DPP-IV (16.36%) and exhibited the highest antioxidant capacity (ORAC: 0.75 μM TE/μM peptide). Conversely, QDQHQKIR demonstrated the highest α-amylase inhibition (18.43%) and Cu2+ chelation (40.4%), supporting its role in carbohydrate metabolism and metal-ion homeostasis. Overall, NIYQIS emerged as the most promising peptide, highlighting the potential of quinoa-derived peptides as functional ingredients to mitigate oxidative stress and metabolic disorders.