GdTI, the first thermostable trypsin inhibitor from Geoffroea decorticans seeds : A novel natural drug with potential application in biomedicine
- Autores
- Cotabarren, Juliana; Broitman, Daiana Judith; Quiroga, Evelina; Obregón, Walter David
- Año de publicación
- 2020
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- A novel thermostable trypsin inhibitorwas obtained fromGeoffroea decorticans seeds. G. decorticans trypsin inhibitor (GdTI) is a protein with molecular mass of 6743.7 Da, with a potent inhibitory activity (Ki of 2.1 nM) even at high temperatures and extreme pHs (100% after 5 h at 100 °C and 80% after 60 min at pH 2–12) constituting one of the most powerful serine protease inhibitors isolated from a plant source. GdTI displays anticoagulant activity against both extrinsic and intrinsic coagulation pathways, representing the first report of a plant serine protease inhibitor with anticoagulant activity against the extrinsic pathway. Finally, GdTI showed inhibitory activity against α- glucosidase (IC50 of 0.18 μM) evidencing the hypoglycemic effect of this inhibitor. Our results evidence the discovery of a natural molecule with unique features: i) GdTI is one of the most potent serine protease inhibitors founded to date, ii)with themost powerful thermostability reported in literature, iii)with anticoagulant effect against both coagulation pathways and hypoglycemic activity. This report suggest that GdTI could be exploited as a natural and hyperstable antidiabetic drug, in behalf of its antithrombotic and hypoglycemic activities, encouraging future studies with high impact on biomedical research and potential pharmaceutical applications.
Centro de Investigación de Proteínas Vegetales - Materia
-
Biología
Geoffroea decorticans
Trypsin inhibitor
Serine protease inhibitor
Anticoagulant activity - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by/4.0/
- Repositorio
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/164072
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GdTI, the first thermostable trypsin inhibitor from Geoffroea decorticans seeds : A novel natural drug with potential application in biomedicineCotabarren, JulianaBroitman, Daiana JudithQuiroga, EvelinaObregón, Walter DavidBiologíaGeoffroea decorticansTrypsin inhibitorSerine protease inhibitorAnticoagulant activityA novel thermostable trypsin inhibitorwas obtained fromGeoffroea decorticans seeds. G. decorticans trypsin inhibitor (GdTI) is a protein with molecular mass of 6743.7 Da, with a potent inhibitory activity (Ki of 2.1 nM) even at high temperatures and extreme pHs (100% after 5 h at 100 °C and 80% after 60 min at pH 2–12) constituting one of the most powerful serine protease inhibitors isolated from a plant source. GdTI displays anticoagulant activity against both extrinsic and intrinsic coagulation pathways, representing the first report of a plant serine protease inhibitor with anticoagulant activity against the extrinsic pathway. Finally, GdTI showed inhibitory activity against α- glucosidase (IC50 of 0.18 μM) evidencing the hypoglycemic effect of this inhibitor. Our results evidence the discovery of a natural molecule with unique features: i) GdTI is one of the most potent serine protease inhibitors founded to date, ii)with themost powerful thermostability reported in literature, iii)with anticoagulant effect against both coagulation pathways and hypoglycemic activity. This report suggest that GdTI could be exploited as a natural and hyperstable antidiabetic drug, in behalf of its antithrombotic and hypoglycemic activities, encouraging future studies with high impact on biomedical research and potential pharmaceutical applications.Centro de Investigación de Proteínas Vegetales2020info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf869-879http://sedici.unlp.edu.ar/handle/10915/164072enginfo:eu-repo/semantics/altIdentifier/issn/0141-8130info:eu-repo/semantics/altIdentifier/doi/10.1016/j.ijbiomac.2020.01.214info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-03T11:15:06Zoai:sedici.unlp.edu.ar:10915/164072Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 11:15:06.639SEDICI (UNLP) - Universidad Nacional de La Platafalse |
dc.title.none.fl_str_mv |
GdTI, the first thermostable trypsin inhibitor from Geoffroea decorticans seeds : A novel natural drug with potential application in biomedicine |
title |
GdTI, the first thermostable trypsin inhibitor from Geoffroea decorticans seeds : A novel natural drug with potential application in biomedicine |
spellingShingle |
GdTI, the first thermostable trypsin inhibitor from Geoffroea decorticans seeds : A novel natural drug with potential application in biomedicine Cotabarren, Juliana Biología Geoffroea decorticans Trypsin inhibitor Serine protease inhibitor Anticoagulant activity |
title_short |
GdTI, the first thermostable trypsin inhibitor from Geoffroea decorticans seeds : A novel natural drug with potential application in biomedicine |
title_full |
GdTI, the first thermostable trypsin inhibitor from Geoffroea decorticans seeds : A novel natural drug with potential application in biomedicine |
title_fullStr |
GdTI, the first thermostable trypsin inhibitor from Geoffroea decorticans seeds : A novel natural drug with potential application in biomedicine |
title_full_unstemmed |
GdTI, the first thermostable trypsin inhibitor from Geoffroea decorticans seeds : A novel natural drug with potential application in biomedicine |
title_sort |
GdTI, the first thermostable trypsin inhibitor from Geoffroea decorticans seeds : A novel natural drug with potential application in biomedicine |
dc.creator.none.fl_str_mv |
Cotabarren, Juliana Broitman, Daiana Judith Quiroga, Evelina Obregón, Walter David |
author |
Cotabarren, Juliana |
author_facet |
Cotabarren, Juliana Broitman, Daiana Judith Quiroga, Evelina Obregón, Walter David |
author_role |
author |
author2 |
Broitman, Daiana Judith Quiroga, Evelina Obregón, Walter David |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
Biología Geoffroea decorticans Trypsin inhibitor Serine protease inhibitor Anticoagulant activity |
topic |
Biología Geoffroea decorticans Trypsin inhibitor Serine protease inhibitor Anticoagulant activity |
dc.description.none.fl_txt_mv |
A novel thermostable trypsin inhibitorwas obtained fromGeoffroea decorticans seeds. G. decorticans trypsin inhibitor (GdTI) is a protein with molecular mass of 6743.7 Da, with a potent inhibitory activity (Ki of 2.1 nM) even at high temperatures and extreme pHs (100% after 5 h at 100 °C and 80% after 60 min at pH 2–12) constituting one of the most powerful serine protease inhibitors isolated from a plant source. GdTI displays anticoagulant activity against both extrinsic and intrinsic coagulation pathways, representing the first report of a plant serine protease inhibitor with anticoagulant activity against the extrinsic pathway. Finally, GdTI showed inhibitory activity against α- glucosidase (IC50 of 0.18 μM) evidencing the hypoglycemic effect of this inhibitor. Our results evidence the discovery of a natural molecule with unique features: i) GdTI is one of the most potent serine protease inhibitors founded to date, ii)with themost powerful thermostability reported in literature, iii)with anticoagulant effect against both coagulation pathways and hypoglycemic activity. This report suggest that GdTI could be exploited as a natural and hyperstable antidiabetic drug, in behalf of its antithrombotic and hypoglycemic activities, encouraging future studies with high impact on biomedical research and potential pharmaceutical applications. Centro de Investigación de Proteínas Vegetales |
description |
A novel thermostable trypsin inhibitorwas obtained fromGeoffroea decorticans seeds. G. decorticans trypsin inhibitor (GdTI) is a protein with molecular mass of 6743.7 Da, with a potent inhibitory activity (Ki of 2.1 nM) even at high temperatures and extreme pHs (100% after 5 h at 100 °C and 80% after 60 min at pH 2–12) constituting one of the most powerful serine protease inhibitors isolated from a plant source. GdTI displays anticoagulant activity against both extrinsic and intrinsic coagulation pathways, representing the first report of a plant serine protease inhibitor with anticoagulant activity against the extrinsic pathway. Finally, GdTI showed inhibitory activity against α- glucosidase (IC50 of 0.18 μM) evidencing the hypoglycemic effect of this inhibitor. Our results evidence the discovery of a natural molecule with unique features: i) GdTI is one of the most potent serine protease inhibitors founded to date, ii)with themost powerful thermostability reported in literature, iii)with anticoagulant effect against both coagulation pathways and hypoglycemic activity. This report suggest that GdTI could be exploited as a natural and hyperstable antidiabetic drug, in behalf of its antithrombotic and hypoglycemic activities, encouraging future studies with high impact on biomedical research and potential pharmaceutical applications. |
publishDate |
2020 |
dc.date.none.fl_str_mv |
2020 |
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/10915/164072 |
url |
http://sedici.unlp.edu.ar/handle/10915/164072 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/issn/0141-8130 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.ijbiomac.2020.01.214 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International (CC BY 4.0) |
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openAccess |
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http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International (CC BY 4.0) |
dc.format.none.fl_str_mv |
application/pdf 869-879 |
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