Peptide synthesis in aqueous-organic biphasic systems catalyzed by a protease isolated from Morrenia brachysthephana (Asclepiadaceae)

Autores
Barberis, Sonia Esther; Quiroga, Evelina; Arribére, María Cecilia; Priolo, Nora Silvia
Año de publicación
2002
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A new cysteine protease, morrenain b II, isolated from the latex of a South American climbing plant, Morrenia brachystephana Griseb. (Asclepiadaceae), was found to be stable in aqueous–organic biphasic systems. In this work, we have investigated the ability of morrenain b II to perform peptide synthesis using Phe.OMe and Asp as substrates; Cys as activator; 0.1 M Tris–HCl buffer pH 8.5 and chloroform as reaction media. The reaction products were separated by RP-HPLC and identified by TLC, H-NMR and EI-MS. Morrenain b II showed high specificity towards bonds between Cys and Phe.OMe amino acids. A significant amount of the cystine–Phe.OMe peptide was produced within 1 h. These preliminary results were compared with papain under the same conditions.
Fil: Barberis, Sonia Esther. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia. Laboratorio de Bromatología; Argentina
Fil: Quiroga, Evelina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia. Laboratorio de Bromatología; Argentina
Fil: Arribére, María Cecilia. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Priolo, Nora Silvia. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Materia
CYSTEINE PROTEASES
MORRENIA BRACHYSTEPHANA
PEPTIDE SYNTHESIS
NON CONVENTIONAL MEDIA
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/156284
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Peptide synthesis in aqueous-organic biphasic systems catalyzed by a protease isolated from Morrenia brachysthephana (Asclepiadaceae)Barberis, Sonia EstherQuiroga, EvelinaArribére, María CeciliaPriolo, Nora SilviaCYSTEINE PROTEASESMORRENIA BRACHYSTEPHANAPEPTIDE SYNTHESISNON CONVENTIONAL MEDIAhttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2A new cysteine protease, morrenain b II, isolated from the latex of a South American climbing plant, Morrenia brachystephana Griseb. (Asclepiadaceae), was found to be stable in aqueous–organic biphasic systems. In this work, we have investigated the ability of morrenain b II to perform peptide synthesis using Phe.OMe and Asp as substrates; Cys as activator; 0.1 M Tris–HCl buffer pH 8.5 and chloroform as reaction media. The reaction products were separated by RP-HPLC and identified by TLC, H-NMR and EI-MS. Morrenain b II showed high specificity towards bonds between Cys and Phe.OMe amino acids. A significant amount of the cystine–Phe.OMe peptide was produced within 1 h. These preliminary results were compared with papain under the same conditions.Fil: Barberis, Sonia Esther. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia. Laboratorio de Bromatología; ArgentinaFil: Quiroga, Evelina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia. Laboratorio de Bromatología; ArgentinaFil: Arribére, María Cecilia. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; ArgentinaFil: Priolo, Nora Silvia. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; ArgentinaElsevier Science2002-03-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/156284Barberis, Sonia Esther; Quiroga, Evelina; Arribére, María Cecilia; Priolo, Nora Silvia; Peptide synthesis in aqueous-organic biphasic systems catalyzed by a protease isolated from Morrenia brachysthephana (Asclepiadaceae); Elsevier Science; Journal of Molecular Catalysis B: Enzymatic; 17; 1; 7-3-2002; 39-471381-1177CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S1381117701000789info:eu-repo/semantics/altIdentifier/doi/10.1016/S1381-1177(01)00078-9info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:31:00Zoai:ri.conicet.gov.ar:11336/156284instacron: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:34982025-10-15 15:31:00.837CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Peptide synthesis in aqueous-organic biphasic systems catalyzed by a protease isolated from Morrenia brachysthephana (Asclepiadaceae)
title Peptide synthesis in aqueous-organic biphasic systems catalyzed by a protease isolated from Morrenia brachysthephana (Asclepiadaceae)
spellingShingle Peptide synthesis in aqueous-organic biphasic systems catalyzed by a protease isolated from Morrenia brachysthephana (Asclepiadaceae)
Barberis, Sonia Esther
CYSTEINE PROTEASES
MORRENIA BRACHYSTEPHANA
PEPTIDE SYNTHESIS
NON CONVENTIONAL MEDIA
title_short Peptide synthesis in aqueous-organic biphasic systems catalyzed by a protease isolated from Morrenia brachysthephana (Asclepiadaceae)
title_full Peptide synthesis in aqueous-organic biphasic systems catalyzed by a protease isolated from Morrenia brachysthephana (Asclepiadaceae)
title_fullStr Peptide synthesis in aqueous-organic biphasic systems catalyzed by a protease isolated from Morrenia brachysthephana (Asclepiadaceae)
title_full_unstemmed Peptide synthesis in aqueous-organic biphasic systems catalyzed by a protease isolated from Morrenia brachysthephana (Asclepiadaceae)
title_sort Peptide synthesis in aqueous-organic biphasic systems catalyzed by a protease isolated from Morrenia brachysthephana (Asclepiadaceae)
dc.creator.none.fl_str_mv Barberis, Sonia Esther
Quiroga, Evelina
Arribére, María Cecilia
Priolo, Nora Silvia
author Barberis, Sonia Esther
author_facet Barberis, Sonia Esther
Quiroga, Evelina
Arribére, María Cecilia
Priolo, Nora Silvia
author_role author
author2 Quiroga, Evelina
Arribére, María Cecilia
Priolo, Nora Silvia
author2_role author
author
author
dc.subject.none.fl_str_mv CYSTEINE PROTEASES
MORRENIA BRACHYSTEPHANA
PEPTIDE SYNTHESIS
NON CONVENTIONAL MEDIA
topic CYSTEINE PROTEASES
MORRENIA BRACHYSTEPHANA
PEPTIDE SYNTHESIS
NON CONVENTIONAL MEDIA
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv A new cysteine protease, morrenain b II, isolated from the latex of a South American climbing plant, Morrenia brachystephana Griseb. (Asclepiadaceae), was found to be stable in aqueous–organic biphasic systems. In this work, we have investigated the ability of morrenain b II to perform peptide synthesis using Phe.OMe and Asp as substrates; Cys as activator; 0.1 M Tris–HCl buffer pH 8.5 and chloroform as reaction media. The reaction products were separated by RP-HPLC and identified by TLC, H-NMR and EI-MS. Morrenain b II showed high specificity towards bonds between Cys and Phe.OMe amino acids. A significant amount of the cystine–Phe.OMe peptide was produced within 1 h. These preliminary results were compared with papain under the same conditions.
Fil: Barberis, Sonia Esther. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia. Laboratorio de Bromatología; Argentina
Fil: Quiroga, Evelina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia. Laboratorio de Bromatología; Argentina
Fil: Arribére, María Cecilia. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Priolo, Nora Silvia. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
description A new cysteine protease, morrenain b II, isolated from the latex of a South American climbing plant, Morrenia brachystephana Griseb. (Asclepiadaceae), was found to be stable in aqueous–organic biphasic systems. In this work, we have investigated the ability of morrenain b II to perform peptide synthesis using Phe.OMe and Asp as substrates; Cys as activator; 0.1 M Tris–HCl buffer pH 8.5 and chloroform as reaction media. The reaction products were separated by RP-HPLC and identified by TLC, H-NMR and EI-MS. Morrenain b II showed high specificity towards bonds between Cys and Phe.OMe amino acids. A significant amount of the cystine–Phe.OMe peptide was produced within 1 h. These preliminary results were compared with papain under the same conditions.
publishDate 2002
dc.date.none.fl_str_mv 2002-03-07
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/11336/156284
Barberis, Sonia Esther; Quiroga, Evelina; Arribére, María Cecilia; Priolo, Nora Silvia; Peptide synthesis in aqueous-organic biphasic systems catalyzed by a protease isolated from Morrenia brachysthephana (Asclepiadaceae); Elsevier Science; Journal of Molecular Catalysis B: Enzymatic; 17; 1; 7-3-2002; 39-47
1381-1177
CONICET Digital
CONICET
url http://hdl.handle.net/11336/156284
identifier_str_mv Barberis, Sonia Esther; Quiroga, Evelina; Arribére, María Cecilia; Priolo, Nora Silvia; Peptide synthesis in aqueous-organic biphasic systems catalyzed by a protease isolated from Morrenia brachysthephana (Asclepiadaceae); Elsevier Science; Journal of Molecular Catalysis B: Enzymatic; 17; 1; 7-3-2002; 39-47
1381-1177
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.sciencedirect.com/science/article/abs/pii/S1381117701000789
info:eu-repo/semantics/altIdentifier/doi/10.1016/S1381-1177(01)00078-9
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
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_ 1846083447042342912
score 13.221938

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