GdTI, the first thermostable trypsin inhibitor from Geoffroea decorticans seeds : A novel natural drug with potential application in biomedicine

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% afte...

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Autores principales: Cotabarren, Juliana, Broitman, Daiana Judith, Quiroga, Evelina, Obregón, Walter David
Formato: Articulo
Lenguaje:Inglés
Publicado: 2020
Materias:
Biología
Geoffroea decorticans
Trypsin inhibitor
Serine protease inhibitor
Anticoagulant activity
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/164072
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-164072
record_format dspace
spelling I19-R120-10915-1640722024-03-20T20:09:54Z http://sedici.unlp.edu.ar/handle/10915/164072 GdTI, the first thermostable trypsin inhibitor from Geoffroea decorticans seeds : A novel natural drug with potential application in biomedicine Cotabarren, Juliana Broitman, Daiana Judith Quiroga, Evelina Obregón, Walter David 2020 2024-03-20T17:27:34Z en Biología Geoffroea decorticans Trypsin inhibitor Serine protease inhibitor Anticoagulant activity 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 Articulo Articulo http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International (CC BY 4.0) application/pdf 869-879
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Biología
Geoffroea decorticans
Trypsin inhibitor
Serine protease inhibitor
Anticoagulant activity
spellingShingle Biología
Geoffroea decorticans
Trypsin inhibitor
Serine protease inhibitor
Anticoagulant activity
Cotabarren, Juliana
Broitman, Daiana Judith
Quiroga, Evelina
Obregón, Walter David
GdTI, the first thermostable trypsin inhibitor from Geoffroea decorticans seeds : A novel natural drug with potential application in biomedicine
topic_facet Biología
Geoffroea decorticans
Trypsin inhibitor
Serine protease inhibitor
Anticoagulant activity
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.
format Articulo
Articulo
author Cotabarren, Juliana
Broitman, Daiana Judith
Quiroga, Evelina
Obregón, Walter David
author_facet Cotabarren, Juliana
Broitman, Daiana Judith
Quiroga, Evelina
Obregón, Walter David
author_sort Cotabarren, Juliana
title GdTI, the first thermostable trypsin inhibitor from Geoffroea decorticans seeds : A novel natural drug with potential application in biomedicine
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
publishDate 2020
url http://sedici.unlp.edu.ar/handle/10915/164072
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