Purification and identification of novel antioxidant peptides isolated from geoffroea decorticans seeds with anticoagulant activity
- Autores
- Cotabarren, Juliana; Ozón, Brenda; Claver, Santiago; Garcia Pardo, Javier; Obregon, Walter David
- Año de publicación
- 2021
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Geoffroea decorticans is a xerophilous deciduous tree present in most arid forests of southern South America, which is commonly used in traditional medicine. The seeds of this tree have been previously investigated for their singular chemical composition, but their protein content has been poorly investigated. Herein, we report the isolation, purification, and characterization of a set of thermostable peptides derived from Geoffroea decorticans seeds (GdAPs) with strong antioxidant and anticoagulant activities. The most potent antioxidant peptides showed a half maximal inhibitory concentration (IC50 ) of 35.5 ± 0.3 µg/mL determined by 1,1-diphenyl-2-picrylhydrazyl (DPPH). They also caused a dose-dependent prolongation of the aPTT clotting time with an IC50 value of ~82 µg/mL. Interestingly, MALDI-TOF/MS analysis showed the presence of three major peptides with low molecular weights of 2257.199 Da, 2717.165 Da, and 5422.002 Da. The derived amino-acid sequence of GdAPs revealed their unique structural features, exhibiting homology with various proteins present in the genome of Arachis hypogaea. All in all, our data suggest a direct applicability of GdAPs for pharmaceutical purposes.
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: Ozón, Brenda. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; 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: Garcia Pardo, Javier. Universitat Autònoma de Barcelona; España
Fil: Obregon, Walter David. 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 - Materia
-
ANTICOAGULANT
ANTIOXIDANT
BIOACTIVE COMPOUND
FUNCTIONAL COMPOUND
GEOFFROEA DECORTICANS
REACTIVE OXYGEN SPECIES
THERMOSTABLE PROTEIN - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/167236
Ver los metadatos del registro completo
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CONICET Digital (CONICET) |
spelling |
Purification and identification of novel antioxidant peptides isolated from geoffroea decorticans seeds with anticoagulant activityCotabarren, JulianaOzón, BrendaClaver, SantiagoGarcia Pardo, JavierObregon, Walter DavidANTICOAGULANTANTIOXIDANTBIOACTIVE COMPOUNDFUNCTIONAL COMPOUNDGEOFFROEA DECORTICANSREACTIVE OXYGEN SPECIESTHERMOSTABLE PROTEINhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Geoffroea decorticans is a xerophilous deciduous tree present in most arid forests of southern South America, which is commonly used in traditional medicine. The seeds of this tree have been previously investigated for their singular chemical composition, but their protein content has been poorly investigated. Herein, we report the isolation, purification, and characterization of a set of thermostable peptides derived from Geoffroea decorticans seeds (GdAPs) with strong antioxidant and anticoagulant activities. The most potent antioxidant peptides showed a half maximal inhibitory concentration (IC50 ) of 35.5 ± 0.3 µg/mL determined by 1,1-diphenyl-2-picrylhydrazyl (DPPH). They also caused a dose-dependent prolongation of the aPTT clotting time with an IC50 value of ~82 µg/mL. Interestingly, MALDI-TOF/MS analysis showed the presence of three major peptides with low molecular weights of 2257.199 Da, 2717.165 Da, and 5422.002 Da. The derived amino-acid sequence of GdAPs revealed their unique structural features, exhibiting homology with various proteins present in the genome of Arachis hypogaea. All in all, our data suggest a direct applicability of GdAPs for pharmaceutical purposes.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: Ozón, Brenda. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; ArgentinaFil: Claver, Santiago. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; ArgentinaFil: Garcia Pardo, Javier. Universitat Autònoma de Barcelona; EspañaFil: Obregon, Walter David. 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; ArgentinaMultidisciplinary Digital Publishing Institute2021-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/167236Cotabarren, Juliana; Ozón, Brenda; Claver, Santiago; Garcia Pardo, Javier; Obregon, Walter David; Purification and identification of novel antioxidant peptides isolated from geoffroea decorticans seeds with anticoagulant activity; Multidisciplinary Digital Publishing Institute; Pharmaceutics; 13; 8; 8-2021; 1-121999-4923CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/1999-4923/13/8/1153info:eu-repo/semantics/altIdentifier/doi/10.3390/pharmaceutics13081153info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:42:01Zoai:ri.conicet.gov.ar:11336/167236instacron: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:34982025-09-29 09:42:01.59CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Purification and identification of novel antioxidant peptides isolated from geoffroea decorticans seeds with anticoagulant activity |
title |
Purification and identification of novel antioxidant peptides isolated from geoffroea decorticans seeds with anticoagulant activity |
spellingShingle |
Purification and identification of novel antioxidant peptides isolated from geoffroea decorticans seeds with anticoagulant activity Cotabarren, Juliana ANTICOAGULANT ANTIOXIDANT BIOACTIVE COMPOUND FUNCTIONAL COMPOUND GEOFFROEA DECORTICANS REACTIVE OXYGEN SPECIES THERMOSTABLE PROTEIN |
title_short |
Purification and identification of novel antioxidant peptides isolated from geoffroea decorticans seeds with anticoagulant activity |
title_full |
Purification and identification of novel antioxidant peptides isolated from geoffroea decorticans seeds with anticoagulant activity |
title_fullStr |
Purification and identification of novel antioxidant peptides isolated from geoffroea decorticans seeds with anticoagulant activity |
title_full_unstemmed |
Purification and identification of novel antioxidant peptides isolated from geoffroea decorticans seeds with anticoagulant activity |
title_sort |
Purification and identification of novel antioxidant peptides isolated from geoffroea decorticans seeds with anticoagulant activity |
dc.creator.none.fl_str_mv |
Cotabarren, Juliana Ozón, Brenda Claver, Santiago Garcia Pardo, Javier Obregon, Walter David |
author |
Cotabarren, Juliana |
author_facet |
Cotabarren, Juliana Ozón, Brenda Claver, Santiago Garcia Pardo, Javier Obregon, Walter David |
author_role |
author |
author2 |
Ozón, Brenda Claver, Santiago Garcia Pardo, Javier Obregon, Walter David |
author2_role |
author author author author |
dc.subject.none.fl_str_mv |
ANTICOAGULANT ANTIOXIDANT BIOACTIVE COMPOUND FUNCTIONAL COMPOUND GEOFFROEA DECORTICANS REACTIVE OXYGEN SPECIES THERMOSTABLE PROTEIN |
topic |
ANTICOAGULANT ANTIOXIDANT BIOACTIVE COMPOUND FUNCTIONAL COMPOUND GEOFFROEA DECORTICANS REACTIVE OXYGEN SPECIES THERMOSTABLE PROTEIN |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Geoffroea decorticans is a xerophilous deciduous tree present in most arid forests of southern South America, which is commonly used in traditional medicine. The seeds of this tree have been previously investigated for their singular chemical composition, but their protein content has been poorly investigated. Herein, we report the isolation, purification, and characterization of a set of thermostable peptides derived from Geoffroea decorticans seeds (GdAPs) with strong antioxidant and anticoagulant activities. The most potent antioxidant peptides showed a half maximal inhibitory concentration (IC50 ) of 35.5 ± 0.3 µg/mL determined by 1,1-diphenyl-2-picrylhydrazyl (DPPH). They also caused a dose-dependent prolongation of the aPTT clotting time with an IC50 value of ~82 µg/mL. Interestingly, MALDI-TOF/MS analysis showed the presence of three major peptides with low molecular weights of 2257.199 Da, 2717.165 Da, and 5422.002 Da. The derived amino-acid sequence of GdAPs revealed their unique structural features, exhibiting homology with various proteins present in the genome of Arachis hypogaea. All in all, our data suggest a direct applicability of GdAPs for pharmaceutical purposes. 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: Ozón, Brenda. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; 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: Garcia Pardo, Javier. Universitat Autònoma de Barcelona; España Fil: Obregon, Walter David. 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 |
description |
Geoffroea decorticans is a xerophilous deciduous tree present in most arid forests of southern South America, which is commonly used in traditional medicine. The seeds of this tree have been previously investigated for their singular chemical composition, but their protein content has been poorly investigated. Herein, we report the isolation, purification, and characterization of a set of thermostable peptides derived from Geoffroea decorticans seeds (GdAPs) with strong antioxidant and anticoagulant activities. The most potent antioxidant peptides showed a half maximal inhibitory concentration (IC50 ) of 35.5 ± 0.3 µg/mL determined by 1,1-diphenyl-2-picrylhydrazyl (DPPH). They also caused a dose-dependent prolongation of the aPTT clotting time with an IC50 value of ~82 µg/mL. Interestingly, MALDI-TOF/MS analysis showed the presence of three major peptides with low molecular weights of 2257.199 Da, 2717.165 Da, and 5422.002 Da. The derived amino-acid sequence of GdAPs revealed their unique structural features, exhibiting homology with various proteins present in the genome of Arachis hypogaea. All in all, our data suggest a direct applicability of GdAPs for pharmaceutical purposes. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-08 |
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/11336/167236 Cotabarren, Juliana; Ozón, Brenda; Claver, Santiago; Garcia Pardo, Javier; Obregon, Walter David; Purification and identification of novel antioxidant peptides isolated from geoffroea decorticans seeds with anticoagulant activity; Multidisciplinary Digital Publishing Institute; Pharmaceutics; 13; 8; 8-2021; 1-12 1999-4923 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/167236 |
identifier_str_mv |
Cotabarren, Juliana; Ozón, Brenda; Claver, Santiago; Garcia Pardo, Javier; Obregon, Walter David; Purification and identification of novel antioxidant peptides isolated from geoffroea decorticans seeds with anticoagulant activity; Multidisciplinary Digital Publishing Institute; Pharmaceutics; 13; 8; 8-2021; 1-12 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/url/https://www.mdpi.com/1999-4923/13/8/1153 info:eu-repo/semantics/altIdentifier/doi/10.3390/pharmaceutics13081153 |
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 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 |
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1844613324644286464 |
score |
13.070432 |