%0 Journal Article 
%A Marina Alegre, María Luisa
%A Orellana Muriana, José María
%A Vásquez Villanueva, Romy Ángela
%A García López, María Concepción
%T Isolation and characterization of angiotensin converting enzyme inhibitory peptides from peach seed hydrolysates: in vivo assessment of antihypertensive activity
%D 2019
%@ 0021-8561
%U http://hdl.handle.net/10017/44648
%X 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.
%K peach seed hydrolysate
%K ACE-inhibitory peptides
%K cytotoxic assay
%K in vivo assay
%K hypertension
%K chromatography
%K mass spectrometry
%K Química
%K Chemistry
%~ Biblioteca Universidad de Alcala