Isolation and characterization of angiotensin converting enzyme inhibitory peptides from peach seed hydrolysates: in vivo assessment of antihypertensive activity
Authors
Marina Alegre, María Luisa; Orellana Muriana, José María; Vásquez Villanueva, Romy Ángela; García López, María ConcepciónIdentifiers
Permanent link (URI): http://hdl.handle.net/10017/44648DOI: 10.1021/acs.jafc.9b02213
ISSN: 0021-8561
Date
2019-09-18Affiliation
Universidad de Alcalá. Departamento de Química Analítica, Química Física e Ingeniería QuímicaBibliographic citation
Journal of Agricultural and Food Chemistry, 2019, v. 67, n. 37, p. 10313-10320
Keywords
peach seed hydrolysate
ACE-inhibitory peptides
cytotoxic assay
in vivo assay
hypertension
chromatography
mass spectrometry
Project
info:eu-repo/grantAgreement/CAM//S2018%2FBAA-4393/ES/ESTRATEGIAS INTEGRADAS PARA LA MEJORA DE LA CALIDAD, LA SEGURIDAD Y LA FUNCIONALIDAD DE LOS ALIMENTOS: HACIA UNA ALIMENTACIÓN SALUDABLE/AVANSECAL-II
info:eu-repo/grantAgreement/MINECO//AGL2016-79010-R/ES/DESARROLLO DE METODOS SOSTENIBLES PARA EL APROVECHAMIENTO DE SUBPRODUCTOS DE LA INDUSTRIA ALIMENTARIA CON ELEVADO CONTENIDO PROTEICO
Document type
info:eu-repo/semantics/article
Version
info:eu-repo/semantics/publishedVersion
Rights
Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
© ACS
Access rights
info:eu-repo/semantics/openAccess
Abstract
A peptide fraction with molecular masses below 3 kDa (PSH-3 kDa) from a peach seed hydrolysate demonstrated high angiotensin converting enzyme (ACE) inhibitory activity (concentration to inhibit 50% ACE (IC50) = 16.4 mu g/mL) in our previous work. This work proposes a further study of this highly active fraction. RP-HPLC enabled two fractions (F3 and F4) with high inhibitory activity (IC50 = 2.0 +/- 0.5 and 1.2 +/- 0.2 mu g/mL, respectively) to be isolated. Peptide analysis by LC-Q-TOF-MS/MS using reverse-phase and hydrophilic interaction chromatography enabled 33 peptides within both fractions to be identified. Among them, peptide isoleucine-tyrosine-serine-proline-histidine (IYSPH) showed the highest capacity. The lack of cytotoxicity of peptides was demonstrated in three different cell lines (HeLa, HT-29, and HK-2). Oral administration of PSH-3 kDa fraction or peptide IYSPH caused a significant systolic blood pressure reduction (-30 mmHg) on spontaneously hypertensive rats after 3-6 h treatment.
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