In vitro inhibition of dipeptidyl peptidase IV by peptides derived from the hydrolysis of amaranth (Amaranthus hypochondriacus L.) proteins

• Published in: Food chemistry Vol. 136; no. 2; pp. 758 - 764
• Main Authors: Velarde-Salcedo, Aída J., Barrera-Pacheco, Alberto, Lara-González, Samuel, Montero-Morán, Gabriela M., Díaz-Gois, Agustín, González de Mejia, Elvira, Barba de la Rosa, Ana P.
• Format: Journal Article
• Language: English
• Published: Kidlington Elsevier Ltd 15-01-2013; Elsevier
• Subjects: Amaranthus - chemistry; Amaranthus - genetics; Amaranthus hypochondriacus; Amino Acid Sequence; Animals; Biological and medical sciences; Catalytic Domain; Cereal and baking product industries; Diabetes; Digestion; Dipeptidyl Peptidase 4 - chemistry; Dipeptidyl peptidase IV; Dipeptidyl-Peptidase IV Inhibitors - chemistry; Dipeptidyl-Peptidase IV Inhibitors - isolation & purification; Docking modeling; Encrypted peptides; Food industries; Fundamental and applied biological sciences. Psychology; Humans; Hydrolysis; Models, Biological; Molecular Sequence Data; Peptides - chemistry; Peptides - genetics; Peptides - isolation & purification; Plant Proteins - chemistry; Plant Proteins - genetics; Seeds - chemistry; Swine; Encrypted peptides; Dipeptidyl peptidase IV; Diabetes; Docking modeling; Amaranthus hypochondriacus; Peptides; Enzyme; Amaranthaceae; In vitro; Modeling; Protein; Hydrolysis; Peptidases; Amaranth; Pseudocereals; Dicotyledones; Angiospermae; Amaranthus; Hydrolases; Spermatophyta; Inhibition
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/j.foodchem.2012.08.032

► Amaranth is an excellent source of peptides with inhibitory activity of DPPIV. ► Amaranth peptides presented up to 50% inhibition of DPPIV activity. ► Glutelins fraction contains peptides such as IPI known as diprotin A. ► Docking models showed the possible mechanism of action of amaranth peptides.
Bioactive compounds present in foods could potentially have beneficial effects on human health. In this study we report the in vitro inhibitory capacity of peptides released from amaranth seed proteins after enzymatic digestion, against dipeptidyl peptidase IV (DPPIV); an enzyme known to deactivate incretins, hormones involved in insulin secretion. Other seeds, such as soybean, black bean, and wheat were also tested. The highest inhibition of DPPIV was observed with amaranth peptides released after simulated gastrointestinal digestion, showing an IC50 of 1.1mg/mL in a dose-dependent manner. In silico tryptic digestion of amaranth globulins was carried out releasing peptides larger than 13 residues. Some of these peptides were used for the in silico prediction of their binding modes with DPPIV. Docking models showed that the possible mechanism of globulin peptides to inhibit DPPIV was through blocking the active dimer formation. Peptides were also found inside the major cavity where the natural substrates reach the catalytic site of the enzyme. This is the first report of the identification of inhibitory DPPIV peptides from amaranth hydrolysates and the prediction of their binding modes at the molecular level, leading to their possible use as functional food ingredients in the prevention of diabetes.