Identification of renin inhibitors peptides from amaranth proteins by docking protocols

Autores
Nardo, Agustina Estefanía; Añón, María Cristina; Quiroga, Alejandra Viviana
Año de publicación
2020
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The 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.
Centro de Investigación y Desarrollo en Criotecnología de Alimentos
Materia
Química
Docking
Renin
Bioactive peptide
Amaranth
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-nd/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/119502
Acceder
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oai_identifier_str oai:sedici.unlp.edu.ar:10915/119502
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Identification of renin inhibitors peptides from amaranth proteins by docking protocolsNardo, Agustina EstefaníaAñón, María CristinaQuiroga, Alejandra VivianaQuímicaDockingReninBioactive peptideAmaranthThe 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.Centro de Investigación y Desarrollo en Criotecnología de Alimentos2020-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://sedici.unlp.edu.ar/handle/10915/119502enginfo:eu-repo/semantics/altIdentifier/issn/1756-4646info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jff.2019.103683info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-nd/4.0/Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-03T11:00:20Zoai:sedici.unlp.edu.ar:10915/119502Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 11:00:21.026SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Identification of renin inhibitors peptides from amaranth proteins by docking protocols
title Identification of renin inhibitors peptides from amaranth proteins by docking protocols
spellingShingle Identification of renin inhibitors peptides from amaranth proteins by docking protocols
Nardo, Agustina Estefanía
Química
Docking
Renin
Bioactive peptide
Amaranth
title_short Identification of renin inhibitors peptides from amaranth proteins by docking protocols
title_full Identification of renin inhibitors peptides from amaranth proteins by docking protocols
title_fullStr Identification of renin inhibitors peptides from amaranth proteins by docking protocols
title_full_unstemmed Identification of renin inhibitors peptides from amaranth proteins by docking protocols
title_sort Identification of renin inhibitors peptides from amaranth proteins by docking protocols
dc.creator.none.fl_str_mv Nardo, Agustina Estefanía
Añón, María Cristina
Quiroga, Alejandra Viviana
author Nardo, Agustina Estefanía
author_facet Nardo, Agustina Estefanía
Añón, María Cristina
Quiroga, Alejandra Viviana
author_role author
author2 Añón, María Cristina
Quiroga, Alejandra Viviana
author2_role author
author
dc.subject.none.fl_str_mv Química
Docking
Renin
Bioactive peptide
Amaranth
topic Química
Docking
Renin
Bioactive peptide
Amaranth
dc.description.none.fl_txt_mv The 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.
Centro de Investigación y Desarrollo en Criotecnología de Alimentos
description The 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.
publishDate 2020
dc.date.none.fl_str_mv 2020-01
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/119502
url http://sedici.unlp.edu.ar/handle/10915/119502
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/1756-4646
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jff.2019.103683
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-nd/4.0/
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-nd/4.0/
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.13397

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