Enzymatic regioselective and complete deacetylation of two arabinonucleosides

Autores
Sabaini, María Belén; Zinni, María A.; Mohorčič, Martina; Friedrich, Jožefa; Iribarren, Adolfo Marcelo; Iglesias, Luis Emilio
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Candida antarctica lipase B (CAL-B)-catalysed regioselective deacetylation of 2′,3′,5′-tri- O-acetyl-1-β- d-arabinofuranosyluracil (1) and 2′,3′,5′-tri- O-acetyl-9-β- d-arabinofuranosyladenine (2) was studied. The choice of the reaction medium allowed the regioselective formation of products bearing different degree of acetylation: in isopropanol, CAL-B catalysed the formation of the corresponding 2′- O-acetylated arabinonucleosides, while hydrolyses afforded the 2′,3′-di- O-acetylated products. In particular, the procedure herein described allows a simple and efficient preparation of the reported vidarabine prodrug 2′,3′-di- O-acetyl-9-β- d-arabinofuranosyladenine, avoiding the utilisation of protective groups. Moreover, to achieve full deacetylation of the assayed substrates, a set of commercial hydrolases and fungal keratinases from Doratomyces microsporus (DMK) and Paecilomyces marquandii (PMK) were tested. While only PMK and DMK catalysed the quantitative complete deacetylation of 1, DMK accomplished full deacetylation of 2 in shorter time than the other assayed enzymes.
Fil: Sabaini, María Belén. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
Fil: Zinni, María A.. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
Fil: Mohorčič, Martina. National Institute Of Chemistry; Eslovenia
Fil: Friedrich, Jožefa. National Institute Of Chemistry; Eslovenia
Fil: Iribarren, Adolfo Marcelo. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
Fil: Iglesias, Luis Emilio. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
Materia
KERATINASE
LIPASE
NUCLEOSIDES
PRODRUGS
REGIOSELECTIVITY
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/190764
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/190764
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Enzymatic regioselective and complete deacetylation of two arabinonucleosidesSabaini, María BelénZinni, María A.Mohorčič, MartinaFriedrich, JožefaIribarren, Adolfo MarceloIglesias, Luis EmilioKERATINASELIPASENUCLEOSIDESPRODRUGSREGIOSELECTIVITYhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Candida antarctica lipase B (CAL-B)-catalysed regioselective deacetylation of 2′,3′,5′-tri- O-acetyl-1-β- d-arabinofuranosyluracil (1) and 2′,3′,5′-tri- O-acetyl-9-β- d-arabinofuranosyladenine (2) was studied. The choice of the reaction medium allowed the regioselective formation of products bearing different degree of acetylation: in isopropanol, CAL-B catalysed the formation of the corresponding 2′- O-acetylated arabinonucleosides, while hydrolyses afforded the 2′,3′-di- O-acetylated products. In particular, the procedure herein described allows a simple and efficient preparation of the reported vidarabine prodrug 2′,3′-di- O-acetyl-9-β- d-arabinofuranosyladenine, avoiding the utilisation of protective groups. Moreover, to achieve full deacetylation of the assayed substrates, a set of commercial hydrolases and fungal keratinases from Doratomyces microsporus (DMK) and Paecilomyces marquandii (PMK) were tested. While only PMK and DMK catalysed the quantitative complete deacetylation of 1, DMK accomplished full deacetylation of 2 in shorter time than the other assayed enzymes.Fil: Sabaini, María Belén. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; ArgentinaFil: Zinni, María A.. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; ArgentinaFil: Mohorčič, Martina. National Institute Of Chemistry; EsloveniaFil: Friedrich, Jožefa. National Institute Of Chemistry; EsloveniaFil: Iribarren, Adolfo Marcelo. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; ArgentinaFil: Iglesias, Luis Emilio. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; ArgentinaElsevier Science2010-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/190764Sabaini, María Belén; Zinni, María A.; Mohorčič, Martina; Friedrich, Jožefa; Iribarren, Adolfo Marcelo; et al.; Enzymatic regioselective and complete deacetylation of two arabinonucleosides; Elsevier Science; Journal of Molecular Catalysis B: Enzymatic; 62; 3-4; 3-2010; 225-2291381-1177CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1381117709002641info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2009.10.011info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:20:10Zoai:ri.conicet.gov.ar:11336/190764instacron: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:34982025-09-10 13:20:10.331CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Enzymatic regioselective and complete deacetylation of two arabinonucleosides
title Enzymatic regioselective and complete deacetylation of two arabinonucleosides
spellingShingle Enzymatic regioselective and complete deacetylation of two arabinonucleosides
Sabaini, María Belén
KERATINASE
LIPASE
NUCLEOSIDES
PRODRUGS
REGIOSELECTIVITY
title_short Enzymatic regioselective and complete deacetylation of two arabinonucleosides
title_full Enzymatic regioselective and complete deacetylation of two arabinonucleosides
title_fullStr Enzymatic regioselective and complete deacetylation of two arabinonucleosides
title_full_unstemmed Enzymatic regioselective and complete deacetylation of two arabinonucleosides
title_sort Enzymatic regioselective and complete deacetylation of two arabinonucleosides
dc.creator.none.fl_str_mv Sabaini, María Belén
Zinni, María A.
Mohorčič, Martina
Friedrich, Jožefa
Iribarren, Adolfo Marcelo
Iglesias, Luis Emilio
author Sabaini, María Belén
author_facet Sabaini, María Belén
Zinni, María A.
Mohorčič, Martina
Friedrich, Jožefa
Iribarren, Adolfo Marcelo
Iglesias, Luis Emilio
author_role author
author2 Zinni, María A.
Mohorčič, Martina
Friedrich, Jožefa
Iribarren, Adolfo Marcelo
Iglesias, Luis Emilio
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv KERATINASE
LIPASE
NUCLEOSIDES
PRODRUGS
REGIOSELECTIVITY
topic KERATINASE
LIPASE
NUCLEOSIDES
PRODRUGS
REGIOSELECTIVITY
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Candida antarctica lipase B (CAL-B)-catalysed regioselective deacetylation of 2′,3′,5′-tri- O-acetyl-1-β- d-arabinofuranosyluracil (1) and 2′,3′,5′-tri- O-acetyl-9-β- d-arabinofuranosyladenine (2) was studied. The choice of the reaction medium allowed the regioselective formation of products bearing different degree of acetylation: in isopropanol, CAL-B catalysed the formation of the corresponding 2′- O-acetylated arabinonucleosides, while hydrolyses afforded the 2′,3′-di- O-acetylated products. In particular, the procedure herein described allows a simple and efficient preparation of the reported vidarabine prodrug 2′,3′-di- O-acetyl-9-β- d-arabinofuranosyladenine, avoiding the utilisation of protective groups. Moreover, to achieve full deacetylation of the assayed substrates, a set of commercial hydrolases and fungal keratinases from Doratomyces microsporus (DMK) and Paecilomyces marquandii (PMK) were tested. While only PMK and DMK catalysed the quantitative complete deacetylation of 1, DMK accomplished full deacetylation of 2 in shorter time than the other assayed enzymes.
Fil: Sabaini, María Belén. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
Fil: Zinni, María A.. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
Fil: Mohorčič, Martina. National Institute Of Chemistry; Eslovenia
Fil: Friedrich, Jožefa. National Institute Of Chemistry; Eslovenia
Fil: Iribarren, Adolfo Marcelo. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
Fil: Iglesias, Luis Emilio. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
description Candida antarctica lipase B (CAL-B)-catalysed regioselective deacetylation of 2′,3′,5′-tri- O-acetyl-1-β- d-arabinofuranosyluracil (1) and 2′,3′,5′-tri- O-acetyl-9-β- d-arabinofuranosyladenine (2) was studied. The choice of the reaction medium allowed the regioselective formation of products bearing different degree of acetylation: in isopropanol, CAL-B catalysed the formation of the corresponding 2′- O-acetylated arabinonucleosides, while hydrolyses afforded the 2′,3′-di- O-acetylated products. In particular, the procedure herein described allows a simple and efficient preparation of the reported vidarabine prodrug 2′,3′-di- O-acetyl-9-β- d-arabinofuranosyladenine, avoiding the utilisation of protective groups. Moreover, to achieve full deacetylation of the assayed substrates, a set of commercial hydrolases and fungal keratinases from Doratomyces microsporus (DMK) and Paecilomyces marquandii (PMK) were tested. While only PMK and DMK catalysed the quantitative complete deacetylation of 1, DMK accomplished full deacetylation of 2 in shorter time than the other assayed enzymes.
publishDate 2010
dc.date.none.fl_str_mv 2010-03
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/11336/190764
Sabaini, María Belén; Zinni, María A.; Mohorčič, Martina; Friedrich, Jožefa; Iribarren, Adolfo Marcelo; et al.; Enzymatic regioselective and complete deacetylation of two arabinonucleosides; Elsevier Science; Journal of Molecular Catalysis B: Enzymatic; 62; 3-4; 3-2010; 225-229
1381-1177
CONICET Digital
CONICET
url http://hdl.handle.net/11336/190764
identifier_str_mv Sabaini, María Belén; Zinni, María A.; Mohorčič, Martina; Friedrich, Jožefa; Iribarren, Adolfo Marcelo; et al.; Enzymatic regioselective and complete deacetylation of two arabinonucleosides; Elsevier Science; Journal of Molecular Catalysis B: Enzymatic; 62; 3-4; 3-2010; 225-229
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/pii/S1381117709002641
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2009.10.011
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv 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_ 1842981105040359424
score 12.48226

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