Bioactive Peptides Originating from Gastrointestinal Endogenous Proteins in the Growing Pig: In Vivo Identification
| Autor: | Paul J. Moughan, Carlos A. Montoya, Lakshmi A. Dave, Maria Hayes, Shane M. Rutherfurd, Leticia Mora |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
DPPH
Swine Serum albumin Peptide Angiotensin-Converting Enzyme Inhibitors Peptidyl-Dipeptidase A 01 natural sciences Antioxidants Lipid peroxidation 03 medical and health sciences chemistry.chemical_compound In vivo Drug Discovery medicine Animals 030304 developmental biology Pharmacology chemistry.chemical_classification 0303 health sciences biology Human serum albumin In vitro 0104 chemical sciences Gastrointestinal Tract 010404 medicinal & biomolecular chemistry Enzyme chemistry Biochemistry biology.protein Peptides medicine.drug |
| Zdroj: | Current pharmaceutical design. 27(11) |
| ISSN: | 1873-4286 |
| Popis: | Background: Recent in silico and in vitro studies have shown that gastrointestinal endogenous proteins (GEP) are a source of bioactive peptides. To date, however, the presence of such peptides in the lumen of the digestive tract has not been demonstrated. Objective: We investigated the generation of GEP-derived bioactive peptides in the growing pig fed a proteinfree diet. Methods: Stomach chyme (SC) and jejunal digesta (JD) fractions from 6 growing pigs (two sampling times) were assessed for their angiotensin-I-converting enzyme (ACE-I; EC 3.4.15.1) inhibition, and antioxidant activity using the 2,2-diphenyl-1-picrylhydrazyl (DPPH) inhibition, ferric reducing antioxidant power (FRAP) and microsomal lipid peroxidation (MLP) inhibition assays. Results: Two of the fractions prepared from JD samples inhibited ACE-I and DPPH by 81 (± 2.80)% and 94 (±0.66)%. SC fractions were found to inhibit MLP between 15-39 (±3.52-1.40)%. The study identified over 180 novel peptide sequences that were related to the determined bioactivities, including a porcine serum albuminderived peptide (FAKTCVADESAENCDKS), corresponding to f(7-23) of the human serum albumin peptide LVNEVTEFAKTCVADESAENCDKSLHTLF that was previously identified from the digests of the latter GEP. Conclusions: This study provides the first in vivo evidence for GEP as a source of bioactive peptides. These new findings help advance our knowledge of the latent bioactive role of GEP-derived peptides in mammalian nutrition and health and their potential pharmaceutical applications. |
| Databáze: | OpenAIRE |
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