Identification of renin inhibitors peptides from amaranth proteins by docking protocols

dc.creatorNardo, Agustina Estefanía
dc.creatorAñón, María Cristina
dc.creatorQuiroga, Alejandra Viviana
dc.date2020-01
dc.date2021-05-31T15:13:47Z
dc.date.accessioned2023-07-15T01:52:55Z
dc.date.available2023-07-15T01:52:55Z
dc.identifierhttp://sedici.unlp.edu.ar/handle/10915/119502
dc.identifierissn:1756-4646
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/7459954
dc.descriptionThe objective of this work was to develop a new protocol to predict with greater confidence peptides as potential inhibitors of the renin enzyme. For this, free, friendly and rigorous servers developed specifically for peptides as ligands were used. Six peptides (SFNLPILR; FNLPILR; SFNLPIL; QAFEDGFEWVSFK; AFEDGFEWVSFK and VNVDDPSKA) identified in an amaranth hydrolysate obtained with alcalase (hydrolysis degree 21%±4) were used. Two positive (angiotensinogen and IRLIIVLMPILMA) and one negative (a tridecapeptide of alanine) controls were included in the analysis. A protocol was designed to include two consecutive stages was performed using CABS-dock server (http://biocomp.chem.uw.edu.pl/CABSdock) and FlexPepDock server (http:// flexpepdock.furmanlab.cs.huji.ac.il/). Peptides SFNLPILR, FNLPILR and AFEDGFEWVSFK inhibited the enzyme in vitro. The heptapeptide FNLPILR was the most potent inhibitor, with an IC50 of 0.41 mM.
dc.descriptionCentro de Investigación y Desarrollo en Criotecnología de Alimentos
dc.formatapplication/pdf
dc.languageen
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.rightsCreative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)
dc.subjectQuímica
dc.subjectDocking
dc.subjectRenin
dc.subjectBioactive peptide
dc.subjectAmaranth
dc.titleIdentification of renin inhibitors peptides from amaranth proteins by docking protocols
dc.typeArticulo
dc.typeArticulo


Este ítem pertenece a la siguiente institución