Purification, identification, and in silico screening of a multifunctional octapeptide from semen armeniacae glutelin-2 hydrolysates: restraining mechanisms to Keap1 and ACE, stability, and ferrous-transport efficiency DOI Creative Commons

Ziqing Jin,

Ling Dang,

Yan Li

et al.

Frontiers in Nutrition, Journal Year: 2025, Volume and Issue: 12

Published: April 4, 2025

Introduction Semen armeniacae is a traditional homologous material of medicine and food, but data on its multifunctional peptides are little. Methods In this study, semen glutelin-2 was hydrolyzed by alcalase trypsin assisted with ultrasound. Antihypertensive antioxidant ferrous-binding activity were isolated, identified, in silico screened from the hydrolysates, action mechanisms against Keap1 angiotensin-I-converting enzyme (ACE), gastrointestinal stability, capacity studied. Results discussion After Sephadex G-15 isolation, electrospray ionization mass spectrometry, AHTpin Peptide Ranker database screening, safe octapeptide: Pro-Val-Asp-Phe-Ala-Gly-Phe-Tyr (PVDFAGFY), obtained. The capacities PVDFAGFY to restrain ACE, chelate ferrous ions, quench hydroxyl radical IC 50 :105.61 μmol/L, 11.67 mg/g, 97.67%, respectively. restrained ACE via competitively linking catalytic (His383) and/or crucial binding sites (Gln281, Lys511, Tyr523, Tyr520, or Ala354), it can inhibit Keap1-Nrf2 interaction 6 residues Keap1. Ferrous ions primarily chelated γ -hydroxyl, carboxyl, amino groups ionic forces. Gastrointestinal hydrolysis did not decrease ( p > 0.05). inhibition model altered iron chelation; however, PVDFAGFY-ferrous showed lower ABTS quenching ferric reducing ability than < stability transmembrane absorption increased Thus, may be exploited as ingredients hypotensive, antioxidant, supplementary agents, vivo hypotensive efficiencies need further study.

Language: Английский

Purification, identification, and in silico screening of a multifunctional octapeptide from semen armeniacae glutelin-2 hydrolysates: restraining mechanisms to Keap1 and ACE, stability, and ferrous-transport efficiency DOI Creative Commons

Ziqing Jin,

Ling Dang,

Yan Li

et al.

Frontiers in Nutrition, Journal Year: 2025, Volume and Issue: 12

Published: April 4, 2025

Introduction Semen armeniacae is a traditional homologous material of medicine and food, but data on its multifunctional peptides are little. Methods In this study, semen glutelin-2 was hydrolyzed by alcalase trypsin assisted with ultrasound. Antihypertensive antioxidant ferrous-binding activity were isolated, identified, in silico screened from the hydrolysates, action mechanisms against Keap1 angiotensin-I-converting enzyme (ACE), gastrointestinal stability, capacity studied. Results discussion After Sephadex G-15 isolation, electrospray ionization mass spectrometry, AHTpin Peptide Ranker database screening, safe octapeptide: Pro-Val-Asp-Phe-Ala-Gly-Phe-Tyr (PVDFAGFY), obtained. The capacities PVDFAGFY to restrain ACE, chelate ferrous ions, quench hydroxyl radical IC 50 :105.61 μmol/L, 11.67 mg/g, 97.67%, respectively. restrained ACE via competitively linking catalytic (His383) and/or crucial binding sites (Gln281, Lys511, Tyr523, Tyr520, or Ala354), it can inhibit Keap1-Nrf2 interaction 6 residues Keap1. Ferrous ions primarily chelated γ -hydroxyl, carboxyl, amino groups ionic forces. Gastrointestinal hydrolysis did not decrease ( p > 0.05). inhibition model altered iron chelation; however, PVDFAGFY-ferrous showed lower ABTS quenching ferric reducing ability than < stability transmembrane absorption increased Thus, may be exploited as ingredients hypotensive, antioxidant, supplementary agents, vivo hypotensive efficiencies need further study.

Language: Английский

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