Anti-diabetic properties of brewer’s spent yeast peptides. In vitro, in silico and ex vivo study after simulated gastrointestinal digestion
Metadatos
Mostrar el registro completo del ítemAutor
Aquino, Marilín Estefanía; Drago, Silvina R.; Sánchez De Medina López-Huertas, Fermín; Martínez Augustín, María Olga; Cian, Raúl E.Editorial
Royal Society of Chemistry
Materia
Diabetes Peptides Molecular docking
Fecha
2024-03-07Referencia bibliográfica
Food Funct., 2024,15, 3778-3790
Patrocinador
Agencia Nacional de Promoción Científica y Tecnológica (ANPCyT) - Argentina (Project PICT-2020-Serie A-1985); Agencia Santafesina de Ciencia Tecnología e Innovación – Argentina (Res. 132/23-Project PEICID-2022-133); Ministerio de Ciencia e Innovación MICINN grant no. PID2020-112768RB-I00; Instituto de Salud Carlos III, grant no. PI21/00952; Junta de Andalucía and FEDER Grants A-AGR-468-UGR20 and P20-00695Resumen
Brewer’s spent yeast (BSY) hydrolysates are a source of antidiabetic peptides. Nevertheless, the impact of
in vitro gastrointestinal digestion of BSY derived peptides on diabetes has not been assessed. In this study,
two BSY hydrolysates were obtained (H1 and H2) using β-glucanase and alkaline protease, with either 1 h
or 2 h hydrolysis time for H1 and H2, respectively. These hydrolysates were then subjected to simulated
gastrointestinal digestion (SGID), obtaining dialysates D1 and D2, respectively. BSY hydrolysates inhibited
the activity of α-glucosidase and dipeptidyl peptidase IV (DPP-IV) enzymes. Moreover, although D2 was
inactive against these enzymes, D1 IC50 value was lower than those found for the hydrolysates.
Interestingly, after electrophoretic separation, D1 mannose-linked peptides showed the highest
α-glucosidase inhibitory activity, while non-glycosylated peptides had the highest DPP-IV inhibitory
activity. Kinetic analyses showed a non-competitive mechanism in both cases. After peptide identification,
GILFVGSGVSGGEEGAR and IINEPTAAAIAYGLDK showed the highest in silico anti-diabetic activities
among mannose-linked and non-glycosylated peptides, respectively (AntiDMPpred score: 0.70 and 0.77).
Molecular docking also indicated that these peptides act as non-competitive inhibitors. Finally, an ex vivo
model of mouse jejunum organoids was used to study the effect of D1 on the expression of intestinal epithelial
genes related to diabetes. The reduction of the expression of genes that codify lactase, sucraseisomaltase
and glucose transporter 2 was observed, as well as an increase in the expression of Gip
(glucose-dependent insulinotropic peptide) and Glp1 (glucagon-like peptide 1). This is the first report to
evaluate the anti-diabetic effect of BSY peptides in mouse jejunum organoids