Purification and characterization of a novel thermostable papain inhibitor from Moringa oleifera with antimicrobial and anticoagulant properties

Autores
Cotabarren, Juliana; Claver, Santiago; Abreu Payrol, Juan; Garcia Pardo, Javier; Obregon, Walter David
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Plant cystatins (or phytocystatins) comprise a large superfamily of natural bioactive small proteins that typically act as protein inhibitors of papain-like cysteine proteases. In this report, we present the purification and characterization of the first phytocystatin isolated from Moringa oleifera (MoPI). MoPI has a molecular mass of 19 kDa and showed an extraordinary physicochemical stability against acidic pHs and high temperatures. Our findings also revealed that MoPI is one of the most potent cysteine protease inhibitors reported to date, with Ki and IC50 values of 2.1 nM and 5.7 nM, respectively. More interestingly, MoPI presents a strong antimicrobial activity against human pathogens such as Enterococcus faecalis and Staphylococcus aureus. In addition, MoPI also showed important anticoagulant activity, which is an unprecedented property for this family of protease inhibitors. These results highlight the pharmaceutical potential of this plant and its derived bioactive molecules.
Fil: Cotabarren, Juliana. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Fil: Claver, Santiago. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Abreu Payrol, Juan. Escuela Latinoamericana de Medicina; Cuba. Entidad de Ciencia, Tecnologia e Innovacion Sierra Maestra; Cuba
Fil: Garcia Pardo, Javier. Universitat Autònoma de Barcelona; España
Fil: Obregon, Walter David. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Materia
ANTIBACTERIAL
ANTICOAGULANT
BIOACTIVE COMPOUND
MORINGA OLEIFERA
PAPAIN INHIBITOR
PHYTOCYSTATIN
PLANT PROTEASE INHIBITOR
PROTEASE
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/158516
Acceder
id CONICETDig_4f7da6ebdb98196c181e009150cfc69c
oai_identifier_str oai:ri.conicet.gov.ar:11336/158516
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Purification and characterization of a novel thermostable papain inhibitor from Moringa oleifera with antimicrobial and anticoagulant propertiesCotabarren, JulianaClaver, SantiagoAbreu Payrol, JuanGarcia Pardo, JavierObregon, Walter DavidANTIBACTERIALANTICOAGULANTBIOACTIVE COMPOUNDMORINGA OLEIFERAPAPAIN INHIBITORPHYTOCYSTATINPLANT PROTEASE INHIBITORPROTEASEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Plant cystatins (or phytocystatins) comprise a large superfamily of natural bioactive small proteins that typically act as protein inhibitors of papain-like cysteine proteases. In this report, we present the purification and characterization of the first phytocystatin isolated from Moringa oleifera (MoPI). MoPI has a molecular mass of 19 kDa and showed an extraordinary physicochemical stability against acidic pHs and high temperatures. Our findings also revealed that MoPI is one of the most potent cysteine protease inhibitors reported to date, with Ki and IC50 values of 2.1 nM and 5.7 nM, respectively. More interestingly, MoPI presents a strong antimicrobial activity against human pathogens such as Enterococcus faecalis and Staphylococcus aureus. In addition, MoPI also showed important anticoagulant activity, which is an unprecedented property for this family of protease inhibitors. These results highlight the pharmaceutical potential of this plant and its derived bioactive molecules.Fil: Cotabarren, Juliana. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; ArgentinaFil: Claver, Santiago. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; ArgentinaFil: Abreu Payrol, Juan. Escuela Latinoamericana de Medicina; Cuba. Entidad de Ciencia, Tecnologia e Innovacion Sierra Maestra; CubaFil: Garcia Pardo, Javier. Universitat Autònoma de Barcelona; EspañaFil: Obregon, Walter David. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; ArgentinaMultidisciplinary Digital Publishing Institute2021-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/158516Cotabarren, Juliana; Claver, Santiago; Abreu Payrol, Juan; Garcia Pardo, Javier; Obregon, Walter David; Purification and characterization of a novel thermostable papain inhibitor from Moringa oleifera with antimicrobial and anticoagulant properties; Multidisciplinary Digital Publishing Institute; Pharmaceutics; 13; 4; 4-2021; 1-111999-4923CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.3390/pharmaceutics13040512info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/1999-4923/13/4/512info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:01:03Zoai:ri.conicet.gov.ar:11336/158516instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:01:04.255CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Purification and characterization of a novel thermostable papain inhibitor from Moringa oleifera with antimicrobial and anticoagulant properties
title Purification and characterization of a novel thermostable papain inhibitor from Moringa oleifera with antimicrobial and anticoagulant properties
spellingShingle Purification and characterization of a novel thermostable papain inhibitor from Moringa oleifera with antimicrobial and anticoagulant properties
Cotabarren, Juliana
ANTIBACTERIAL
ANTICOAGULANT
BIOACTIVE COMPOUND
MORINGA OLEIFERA
PAPAIN INHIBITOR
PHYTOCYSTATIN
PLANT PROTEASE INHIBITOR
PROTEASE
title_short Purification and characterization of a novel thermostable papain inhibitor from Moringa oleifera with antimicrobial and anticoagulant properties
title_full Purification and characterization of a novel thermostable papain inhibitor from Moringa oleifera with antimicrobial and anticoagulant properties
title_fullStr Purification and characterization of a novel thermostable papain inhibitor from Moringa oleifera with antimicrobial and anticoagulant properties
title_full_unstemmed Purification and characterization of a novel thermostable papain inhibitor from Moringa oleifera with antimicrobial and anticoagulant properties
title_sort Purification and characterization of a novel thermostable papain inhibitor from Moringa oleifera with antimicrobial and anticoagulant properties
dc.creator.none.fl_str_mv Cotabarren, Juliana
Claver, Santiago
Abreu Payrol, Juan
Garcia Pardo, Javier
Obregon, Walter David
author Cotabarren, Juliana
author_facet Cotabarren, Juliana
Claver, Santiago
Abreu Payrol, Juan
Garcia Pardo, Javier
Obregon, Walter David
author_role author
author2 Claver, Santiago
Abreu Payrol, Juan
Garcia Pardo, Javier
Obregon, Walter David
author2_role author
author
author
author
dc.subject.none.fl_str_mv ANTIBACTERIAL
ANTICOAGULANT
BIOACTIVE COMPOUND
MORINGA OLEIFERA
PAPAIN INHIBITOR
PHYTOCYSTATIN
PLANT PROTEASE INHIBITOR
PROTEASE
topic ANTIBACTERIAL
ANTICOAGULANT
BIOACTIVE COMPOUND
MORINGA OLEIFERA
PAPAIN INHIBITOR
PHYTOCYSTATIN
PLANT PROTEASE INHIBITOR
PROTEASE
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Plant cystatins (or phytocystatins) comprise a large superfamily of natural bioactive small proteins that typically act as protein inhibitors of papain-like cysteine proteases. In this report, we present the purification and characterization of the first phytocystatin isolated from Moringa oleifera (MoPI). MoPI has a molecular mass of 19 kDa and showed an extraordinary physicochemical stability against acidic pHs and high temperatures. Our findings also revealed that MoPI is one of the most potent cysteine protease inhibitors reported to date, with Ki and IC50 values of 2.1 nM and 5.7 nM, respectively. More interestingly, MoPI presents a strong antimicrobial activity against human pathogens such as Enterococcus faecalis and Staphylococcus aureus. In addition, MoPI also showed important anticoagulant activity, which is an unprecedented property for this family of protease inhibitors. These results highlight the pharmaceutical potential of this plant and its derived bioactive molecules.
Fil: Cotabarren, Juliana. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Fil: Claver, Santiago. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Abreu Payrol, Juan. Escuela Latinoamericana de Medicina; Cuba. Entidad de Ciencia, Tecnologia e Innovacion Sierra Maestra; Cuba
Fil: Garcia Pardo, Javier. Universitat Autònoma de Barcelona; España
Fil: Obregon, Walter David. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
description Plant cystatins (or phytocystatins) comprise a large superfamily of natural bioactive small proteins that typically act as protein inhibitors of papain-like cysteine proteases. In this report, we present the purification and characterization of the first phytocystatin isolated from Moringa oleifera (MoPI). MoPI has a molecular mass of 19 kDa and showed an extraordinary physicochemical stability against acidic pHs and high temperatures. Our findings also revealed that MoPI is one of the most potent cysteine protease inhibitors reported to date, with Ki and IC50 values of 2.1 nM and 5.7 nM, respectively. More interestingly, MoPI presents a strong antimicrobial activity against human pathogens such as Enterococcus faecalis and Staphylococcus aureus. In addition, MoPI also showed important anticoagulant activity, which is an unprecedented property for this family of protease inhibitors. These results highlight the pharmaceutical potential of this plant and its derived bioactive molecules.
publishDate 2021
dc.date.none.fl_str_mv 2021-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
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://hdl.handle.net/11336/158516
Cotabarren, Juliana; Claver, Santiago; Abreu Payrol, Juan; Garcia Pardo, Javier; Obregon, Walter David; Purification and characterization of a novel thermostable papain inhibitor from Moringa oleifera with antimicrobial and anticoagulant properties; Multidisciplinary Digital Publishing Institute; Pharmaceutics; 13; 4; 4-2021; 1-11
1999-4923
CONICET Digital
CONICET
url http://hdl.handle.net/11336/158516
identifier_str_mv Cotabarren, Juliana; Claver, Santiago; Abreu Payrol, Juan; Garcia Pardo, Javier; Obregon, Walter David; Purification and characterization of a novel thermostable papain inhibitor from Moringa oleifera with antimicrobial and anticoagulant properties; Multidisciplinary Digital Publishing Institute; Pharmaceutics; 13; 4; 4-2021; 1-11
1999-4923
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.3390/pharmaceutics13040512
info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/1999-4923/13/4/512
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1842269674520182784
score 13.21921

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