Biochemical characterization of the YBPCI miniprotein, the first carboxypeptidase inhibitor isolated from Yellow Bell Pepper (<i>Capsicum annuum</i> L) : A novel contribution to th...

Autores
Cotabarren, Juliana; Tellechea, Mariana Edith; Avilés, Francesc Xavier; Rivera, Julia Lorenzo; Obregón, Walter David
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The cystine-knot metallocarboxypeptidase inhibitors (MCPIs) are peptides that contribute to control proteolytic activity, involved in storage, growth and maintenance of plants. Lately studies reported several MCPIs with potential use in biomedical applications; as anti-cancer, anti-thrombotic, anti-malaric and anti-angiogenic agents. We report the isolation, purification, chemical stability and biochemical characterization of a novel carboxypeptidase A inhibitor (YBPCI) isolated from Capsicum annuum L. var. Yellow Bell Pepper, the first cystine-knot miniprotein (CKM) of the species. We demonstrate the stability of YBPCI (IC50 = 0.90 μg/ml) to high temperatures, high salt concentration and extreme pH values. MALDI-TOF/MS analysis detected a molecular weight of 4057 Da, and peptide mass fingerprint resulted in no matches with other protease inhibitors. In vitro gastrointestinal digestion subjecting YBPCI to pH 2 incubation and proteolytic attack resulted in complete inhibitory activity. To summarize, there are no reports to date of carboxypeptidase inhibitors in C. annuum species, giving our report much more relevance.
Facultad de Ciencias Exactas
Centro de Investigación de Proteínas Vegetales
Materia
Ciencias Exactas
Biología
carboxypeptidase inhibitor
plant inhibitor
Capsicum annuum
protease
stable miniproteins
gastrointestinal digestion
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/108603
Acceder
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oai_identifier_str oai:sedici.unlp.edu.ar:10915/108603
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Biochemical characterization of the YBPCI miniprotein, the first carboxypeptidase inhibitor isolated from Yellow Bell Pepper (<i>Capsicum annuum</i> L) : A novel contribution to the knowledge of miniproteins stabilityCotabarren, JulianaTellechea, Mariana EdithAvilés, Francesc XavierRivera, Julia LorenzoObregón, Walter DavidCiencias ExactasBiologíacarboxypeptidase inhibitorplant inhibitorCapsicum annuumproteasestable miniproteinsgastrointestinal digestionThe cystine-knot metallocarboxypeptidase inhibitors (MCPIs) are peptides that contribute to control proteolytic activity, involved in storage, growth and maintenance of plants. Lately studies reported several MCPIs with potential use in biomedical applications; as anti-cancer, anti-thrombotic, anti-malaric and anti-angiogenic agents. We report the isolation, purification, chemical stability and biochemical characterization of a novel carboxypeptidase A inhibitor (YBPCI) isolated from <i>Capsicum annuum</i> L. var. Yellow Bell Pepper, the first cystine-knot miniprotein (CKM) of the species. We demonstrate the stability of YBPCI (IC50 = 0.90 μg/ml) to high temperatures, high salt concentration and extreme pH values. MALDI-TOF/MS analysis detected a molecular weight of 4057 Da, and peptide mass fingerprint resulted in no matches with other protease inhibitors. <i>In vitro</i> gastrointestinal digestion subjecting YBPCI to pH 2 incubation and proteolytic attack resulted in complete inhibitory activity. To summarize, there are no reports to date of carboxypeptidase inhibitors in <i>C. annuum</i> species, giving our report much more relevance.Facultad de Ciencias ExactasCentro de Investigación de Proteínas Vegetales2018info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf55-61http://sedici.unlp.edu.ar/handle/10915/108603enginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S1046592817306174info:eu-repo/semantics/altIdentifier/issn/1046-5928info:eu-repo/semantics/altIdentifier/doi/10.1016/j.pep.2017.12.003info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:24:37Zoai:sedici.unlp.edu.ar:10915/108603Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:24:37.904SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Biochemical characterization of the YBPCI miniprotein, the first carboxypeptidase inhibitor isolated from Yellow Bell Pepper (<i>Capsicum annuum</i> L) : A novel contribution to the knowledge of miniproteins stability
title Biochemical characterization of the YBPCI miniprotein, the first carboxypeptidase inhibitor isolated from Yellow Bell Pepper (<i>Capsicum annuum</i> L) : A novel contribution to the knowledge of miniproteins stability
spellingShingle Biochemical characterization of the YBPCI miniprotein, the first carboxypeptidase inhibitor isolated from Yellow Bell Pepper (<i>Capsicum annuum</i> L) : A novel contribution to the knowledge of miniproteins stability
Cotabarren, Juliana
Ciencias Exactas
Biología
carboxypeptidase inhibitor
plant inhibitor
Capsicum annuum
protease
stable miniproteins
gastrointestinal digestion
title_short Biochemical characterization of the YBPCI miniprotein, the first carboxypeptidase inhibitor isolated from Yellow Bell Pepper (<i>Capsicum annuum</i> L) : A novel contribution to the knowledge of miniproteins stability
title_full Biochemical characterization of the YBPCI miniprotein, the first carboxypeptidase inhibitor isolated from Yellow Bell Pepper (<i>Capsicum annuum</i> L) : A novel contribution to the knowledge of miniproteins stability
title_fullStr Biochemical characterization of the YBPCI miniprotein, the first carboxypeptidase inhibitor isolated from Yellow Bell Pepper (<i>Capsicum annuum</i> L) : A novel contribution to the knowledge of miniproteins stability
title_full_unstemmed Biochemical characterization of the YBPCI miniprotein, the first carboxypeptidase inhibitor isolated from Yellow Bell Pepper (<i>Capsicum annuum</i> L) : A novel contribution to the knowledge of miniproteins stability
title_sort Biochemical characterization of the YBPCI miniprotein, the first carboxypeptidase inhibitor isolated from Yellow Bell Pepper (<i>Capsicum annuum</i> L) : A novel contribution to the knowledge of miniproteins stability
dc.creator.none.fl_str_mv Cotabarren, Juliana
Tellechea, Mariana Edith
Avilés, Francesc Xavier
Rivera, Julia Lorenzo
Obregón, Walter David
author Cotabarren, Juliana
author_facet Cotabarren, Juliana
Tellechea, Mariana Edith
Avilés, Francesc Xavier
Rivera, Julia Lorenzo
Obregón, Walter David
author_role author
author2 Tellechea, Mariana Edith
Avilés, Francesc Xavier
Rivera, Julia Lorenzo
Obregón, Walter David
author2_role author
author
author
author
dc.subject.none.fl_str_mv Ciencias Exactas
Biología
carboxypeptidase inhibitor
plant inhibitor
Capsicum annuum
protease
stable miniproteins
gastrointestinal digestion
topic Ciencias Exactas
Biología
carboxypeptidase inhibitor
plant inhibitor
Capsicum annuum
protease
stable miniproteins
gastrointestinal digestion
dc.description.none.fl_txt_mv The cystine-knot metallocarboxypeptidase inhibitors (MCPIs) are peptides that contribute to control proteolytic activity, involved in storage, growth and maintenance of plants. Lately studies reported several MCPIs with potential use in biomedical applications; as anti-cancer, anti-thrombotic, anti-malaric and anti-angiogenic agents. We report the isolation, purification, chemical stability and biochemical characterization of a novel carboxypeptidase A inhibitor (YBPCI) isolated from <i>Capsicum annuum</i> L. var. Yellow Bell Pepper, the first cystine-knot miniprotein (CKM) of the species. We demonstrate the stability of YBPCI (IC50 = 0.90 μg/ml) to high temperatures, high salt concentration and extreme pH values. MALDI-TOF/MS analysis detected a molecular weight of 4057 Da, and peptide mass fingerprint resulted in no matches with other protease inhibitors. <i>In vitro</i> gastrointestinal digestion subjecting YBPCI to pH 2 incubation and proteolytic attack resulted in complete inhibitory activity. To summarize, there are no reports to date of carboxypeptidase inhibitors in <i>C. annuum</i> species, giving our report much more relevance.
Facultad de Ciencias Exactas
Centro de Investigación de Proteínas Vegetales
description The cystine-knot metallocarboxypeptidase inhibitors (MCPIs) are peptides that contribute to control proteolytic activity, involved in storage, growth and maintenance of plants. Lately studies reported several MCPIs with potential use in biomedical applications; as anti-cancer, anti-thrombotic, anti-malaric and anti-angiogenic agents. We report the isolation, purification, chemical stability and biochemical characterization of a novel carboxypeptidase A inhibitor (YBPCI) isolated from <i>Capsicum annuum</i> L. var. Yellow Bell Pepper, the first cystine-knot miniprotein (CKM) of the species. We demonstrate the stability of YBPCI (IC50 = 0.90 μg/ml) to high temperatures, high salt concentration and extreme pH values. MALDI-TOF/MS analysis detected a molecular weight of 4057 Da, and peptide mass fingerprint resulted in no matches with other protease inhibitors. <i>In vitro</i> gastrointestinal digestion subjecting YBPCI to pH 2 incubation and proteolytic attack resulted in complete inhibitory activity. To summarize, there are no reports to date of carboxypeptidase inhibitors in <i>C. annuum</i> species, giving our report much more relevance.
publishDate 2018
dc.date.none.fl_str_mv 2018
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/10915/108603
url http://sedici.unlp.edu.ar/handle/10915/108603
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S1046592817306174
info:eu-repo/semantics/altIdentifier/issn/1046-5928
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.pep.2017.12.003
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
55-61
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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