Multifunctionality of lunasin and peptides released during its simulated gastrointestinal digestion.


Journal

Food research international (Ottawa, Ont.)
ISSN: 1873-7145
Titre abrégé: Food Res Int
Pays: Canada
ID NLM: 9210143

Informations de publication

Date de publication:
11 2019
Historique:
received: 30 04 2019
revised: 17 06 2019
accepted: 21 06 2019
entrez: 27 9 2019
pubmed: 27 9 2019
medline: 21 10 2020
Statut: ppublish

Résumé

Oxidative stress, inflammation, and hypertension are recognized risk factors for non-communicable diseases. Because of the preventable character of these factors, the searching of dietary compounds with counteracting effects against them would provide a new framework for the development of novel multifunctional foods or nutraceuticals. Lunasin is a naturally occurring soybean peptide with chemopreventive and anti-inflammatory properties. Upon oral intake, lunasin is susceptible to the action of digestive enzymes during its transit through gastrointestinal tract. In spite of its cleavage into smaller peptides, these fragments have been suggested to contribute on the health beneficial effects attributed to lunasin. To confirm this hypothesis, the multifunctionality of lunasin derived-fragments was investigated. In vitro, peptides corresponding to the N-terminal and central regions of lunasin were demonstrated to inhibit angiotensin converting enzyme and to scavenge peroxyl and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid (ABTS) radicals. Moreover, lunasin and fragments released during its gastrointestinal digestion exerted potent protective effects on cell viability and oxidative status in macrophages RAW264.7 challenged with chemicals tert-butylhydroperoxide and hydrogen peroxide. These peptides were also able to reduce the nitric oxide production in pro-inflammatory lipopolysaccharide-induced macrophages. These results confirm the promising role of lunasin and its derived-fragments as protective agents against oxidative damage and inflammation-associated diseases.

Identifiants

pubmed: 31554062
pii: S0963-9969(19)30384-9
doi: 10.1016/j.foodres.2019.108513
pii:
doi:

Substances chimiques

Anti-Inflammatory Agents 0
Antioxidants 0
GM2S-1 protein, soybean 0
Peptides 0
Soybean Proteins 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

108513

Informations de copyright

Copyright © 2019 Elsevier Ltd. All rights reserved.

Auteurs

Pedro Indiano-Romacho (P)

Instituto de Investigación en Ciencias de la Alimentación (CIAL, CSIC-UAM, CEI UAM+CSIC), Nicolás Cabrera, 9, 28049 Madrid, Spain. Electronic address: pedro.indiano@csic.es.

Samuel Fernández-Tomé (S)

Hospital Universitario de La Princesa and Instituto de Investigación Sanitaria Princesa (IIS-IP), Centro de Investigación Biomédica en Red de Enfermedades Hepáticas y Digestivas (CIBEREHD), Madrid, Spain.

Lourdes Amigo (L)

Instituto de Investigación en Ciencias de la Alimentación (CIAL, CSIC-UAM, CEI UAM+CSIC), Nicolás Cabrera, 9, 28049 Madrid, Spain. Electronic address: lourdes.amigo@csic.es.

Blanca Hernández-Ledesma (B)

Instituto de Investigación en Ciencias de la Alimentación (CIAL, CSIC-UAM, CEI UAM+CSIC), Nicolás Cabrera, 9, 28049 Madrid, Spain. Electronic address: b.hernandez@csic.es.

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Classifications MeSH