Publicaciones

@article{pmid31402656,

title = {Implication of Opioid Receptors in the Antihypertensive Effect of a Bovine Casein Hydrolysate and α-Casein-Derived Peptides},

author = {Laura Sánchez-Rivera and Pedro Ferreira Santos and M Angeles Sevilla and M José Montero and Isidra Recio and Beatriz Miralles},

url = {https://pubs.acs.org/doi/10.1021/acs.jafc.9b03872},

doi = {10.1021/acs.jafc.9b03872},

issn = {1520-5118},

year  = {2020},

date = {2020-02-01},

urldate = {2020-02-01},

journal = {J Agric Food Chem},

volume = {68},

number = {7},

pages = {1877--1883},

abstract = {The antihypertensive activity of two α-casein-derived peptides and casein hydrolysate containing these sequences was evaluated in the presence of naloxone. The activity was abolished by this opioid antagonist at 2, 4, and 6 h post-administration. Similarly, the antihypertensive effect of the α-casein peptides RYLGY (-23.8 ± 2.5 mmHg) and AYFYPEL (-21.1 ± 3.2 mmHg) at 5 mg/kg of body weight was antagonized by the co-administration of naloxone. Because peptide AYFYPEL had recently shown opioid activity, a molecular dynamic simulation of this peptide with human μ-opioid receptor was performed to demonstrate its favorable structure and interaction energy, despite the presence of Ala at the N terminus. Altogether, these results revealed that the  effect on systolic blood pressure of the studied α-casein peptides is mediated by interaction with opioid receptors and the antihypertensive activity of casein hydrolysate can be very likely ascribed to them with the possible contribution of other mechanisms.},

keywords = {antihypertensive peptide, casein hydrolysate, naloxone, opioid receptor, spontaneously hypertensive rat},

pubstate = {published},

tppubtype = {article}

}

@article{SANCHEZRIVERA2016348,

title = {Peptide fragments from β-casein f(134–138), HLPLP, generated by the action of rat blood plasma peptidases show potent antihypertensive activity},

author = {Laura Sánchez-Rivera and Pedro Ferreira Santos and Beatriz Miralles and Rosalía Carrón and M José Montero and Isidra Recio},

url = {https://www.sciencedirect.com/science/article/pii/S0963996915302775},

doi = {https://doi.org/10.1016/j.foodres.2015.12.007},

issn = {0963-9969},

year  = {2016},

date = {2016-01-01},

urldate = {2016-01-01},

journal = {Food Research International},

volume = {88},

pages = {348-353},

abstract = {The intact absorption of a β-casein peptide, HLPLP, into rat blood circulation after oral administration was recently demonstrated. In addition to the parent peptide, several derived fragments were detected in rat plasma. The aim of the present work is to elucidate whether these fragments retain antihypertensive activity and if their activity is mediated by angiotensin-converting-enzyme inhibition. The penta-peptide was incubated in rat plasma in order to identify and quantify the fragments generated by the action of plasmatic peptidases on HLPLP, using tandem mass spectrometry. Peptides HLPL, LPLP and HLP were generated within seconds of incubation. The parent peptide, HLPLP, and all possible derived peptides showed potent antihypertensive activity in spontaneously hypertensive rats and caused inhibition of vascular contraction elicited by angiotensin-I. It can be concluded that the antihypertensive effect of HLPLP can be produced by the concomitant action of the parent peptide and several novel derived fragments.},

note = {The 4th International Conference on Food Digestion},

keywords = {antihypertensive peptide, In vivo active form, Plasma peptidases, SHR, Tandem mass spectrometry},

pubstate = {published},

tppubtype = {article}

}