Human colostrum in vitro protein digestion: peptidomics by liquid chromatography-Orbitrap-high-resolution MS and prospection for bioactive peptides via bioinformatics.

Autor: Campanhon IB; Department of Biochemistry, Institute of Chemistry, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil.; Lipid Biochemistry and Lipidomics Laboratory and Laboratory of Food Science and Nutritional Biochemistry, Institute of Chemistry, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil., de Aguiar PF; Laboratory of Chemometrics (LABQUIM), Department of Analytical Chemistry, Institute of Chemistry, Universidade Federal Rio de Janeiro, Rio de Janeiro, Brazil., Bezerra FF; Department of Basic and Experimental Nutrition, Nutrition Institute, Universidade do Estado do Rio de Janeiro, Rio de Janeiro, Brazil., Soares MR; Department of Biochemistry, Institute of Chemistry, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil., Torres AG; Lipid Biochemistry and Lipidomics Laboratory and Laboratory of Food Science and Nutritional Biochemistry, Institute of Chemistry, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil.
Jazyk: angličtina
Zdroj: The British journal of nutrition [Br J Nutr] 2024 Jan 14; Vol. 131 (1), pp. 17-26. Date of Electronic Publication: 2023 Jul 24.
DOI: 10.1017/S0007114523001459
Abstrakt: Breast milk is known to contain bioactive peptides that are released during digestion, being a major source of bioactive peptides to the new-born, some of which act against invading pathogens. However, the formation of bioactive peptides during digestion of human colostrum remains largely uninvestigated. This study aimed to investigate the formation of peptides during simulated digestion of human colostrum from adult women and to prospect antimicrobial peptides. For this purpose, we used high-resolution MS to monitor the release of peptides during in vitro digestion. Bioinformatics was used for the prospection of antimicrobial activity of peptides. During simulated digestion (oral, gastric and duodenal phases), 2318 peptide sequences derived from 112 precursor proteins were identified. At the end of simulated digestion, casein-derived peptide sequences were the most frequently observed. Among precursors, some proteins were seen for the first time in this study. The resulting peptides were rich in proline, glutamine, valine and leucine residues, providing characteristic traits of antimicrobial peptides. From bioinformatics analysis, seven peptides showed potentially high antimicrobial activity towards bacteria, viruses and fungi, from which the latter was the most prominent predicted activity. Antimicrobial peptides released during digestion may provide a defence platform with controlled release for the new-born.
Databáze: MEDLINE