RT info:eu-repo/semantics/article
T1 Isolation and characterization of angiotensin converting enzyme inhibitory peptides from peach seed hydrolysates: in vivo assessment of antihypertensive activity
A1 Marina Alegre, María Luisa
A1 Orellana Muriana, José María
A1 Vásquez Villanueva, Romy Ángela
A1 García López, María Concepción
K1 peach seed hydrolysate
K1 ACE-inhibitory peptides
K1 cytotoxic assay
K1 in vivo assay
K1 hypertension
K1 chromatography
K1 mass spectrometry
K1 Química
K1 Chemistry
AB 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.
SN 0021-8561
YR 2019
FD 2019-09-18
LK http://hdl.handle.net/10017/44648
UL http://hdl.handle.net/10017/44648
LA eng
DS MINDS@UW
RD 23-abr-2024