An efficient and mild access to N-acetyl protected purine nucleosides based on a chemoselective enzymatic hydrolysis
N-Monoacetylated derivatives of ribo- (adenosine, guanosine) and 2′-deoxyribonucleosides (2′-deoxyadenosine and 2′-deoxyguanosine), useful as oligonucleotide building blocks, were obtained in 88–100% by enzymatic chemoselective hydrolysis of the corresponding peracetylated nucleosides. Among the tes...
| Published in: | Journal of Biotechnology |
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| Main Authors: | , , , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
Elsevier
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| Subjects: | |
| Online Access: | http://hdl.handle.net/11336/24092 |
| _version_ | 1821529798778814464 |
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| author | Palacio, Cyntia M. Sabaini, María Belén Iribarren, Adolfo Marcelo Iglesias, Luis Emilio |
| author_facet | Palacio, Cyntia M. Sabaini, María Belén Iribarren, Adolfo Marcelo Iglesias, Luis Emilio |
| author_sort | Palacio, Cyntia M. |
| collection | CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) |
| container_issue | 2 |
| container_start_page | 99 |
| container_title | Journal of Biotechnology |
| container_volume | 165 |
| description | N-Monoacetylated derivatives of ribo- (adenosine, guanosine) and 2′-deoxyribonucleosides (2′-deoxyadenosine and 2′-deoxyguanosine), useful as oligonucleotide building blocks, were obtained in 88–100% by enzymatic chemoselective hydrolysis of the corresponding peracetylated nucleosides. Among the tested hydrolases, most satisfactory results were found with acylase I from Aspergillus melleus and Candida antarctica lipase B. For acylase I, the observed chemoselectivity towards ester hydrolysis, without amide reaction, broadens the information about the selectivity of the enzyme and its synthetic applications in the field of nucleosides. Fil: Palacio, Cyntia M. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina Fil: Sabaini, María Belén. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina 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. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina |
| format | Article in Journal/Newspaper |
| genre | Antarc* Antarctica |
| genre_facet | Antarc* Antarctica |
| geographic | Argentina Quilmes |
| geographic_facet | Argentina Quilmes |
| id | ftconicet:oai:ri.conicet.gov.ar:11336/24092 |
| institution | Open Polar |
| language | English |
| long_lat | ENVELOPE(-55.617,-55.617,-63.233,-63.233) |
| op_collection_id | ftconicet |
| op_container_end_page | 101 |
| op_doi | https://doi.org/10.1016/j.jbiotec.2013.03.004 |
| op_relation | info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jbiotec.2013.03.004 info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0168165613001399 http://hdl.handle.net/11336/24092 Palacio, Cyntia M.; Sabaini, María Belén; Iribarren, Adolfo Marcelo; Iglesias, Luis Emilio; An efficient and mild access to N-acetyl protected purine nucleosides based on a chemoselective enzymatic hydrolysis; Elsevier; Journal Of Biotechnology; 165; 2; 3-2013; 99-101 0168-1656 CONICET Digital CONICET |
| op_rights | info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
| publisher | Elsevier |
| record_format | openpolar |
| spelling | ftconicet:oai:ri.conicet.gov.ar:11336/24092 2025-01-16T19:02:30+00:00 An efficient and mild access to N-acetyl protected purine nucleosides based on a chemoselective enzymatic hydrolysis Palacio, Cyntia M. Sabaini, María Belén Iribarren, Adolfo Marcelo Iglesias, Luis Emilio application/pdf http://hdl.handle.net/11336/24092 eng eng Elsevier info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jbiotec.2013.03.004 info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0168165613001399 http://hdl.handle.net/11336/24092 Palacio, Cyntia M.; Sabaini, María Belén; Iribarren, Adolfo Marcelo; Iglesias, Luis Emilio; An efficient and mild access to N-acetyl protected purine nucleosides based on a chemoselective enzymatic hydrolysis; Elsevier; Journal Of Biotechnology; 165; 2; 3-2013; 99-101 0168-1656 CONICET Digital CONICET info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ Chemoselectivity Candida Antarctica Lipase B Acylase I Nucleobase N-Protection Oligonucleotide Building Blocks https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion ftconicet https://doi.org/10.1016/j.jbiotec.2013.03.004 2023-09-24T18:37:34Z N-Monoacetylated derivatives of ribo- (adenosine, guanosine) and 2′-deoxyribonucleosides (2′-deoxyadenosine and 2′-deoxyguanosine), useful as oligonucleotide building blocks, were obtained in 88–100% by enzymatic chemoselective hydrolysis of the corresponding peracetylated nucleosides. Among the tested hydrolases, most satisfactory results were found with acylase I from Aspergillus melleus and Candida antarctica lipase B. For acylase I, the observed chemoselectivity towards ester hydrolysis, without amide reaction, broadens the information about the selectivity of the enzyme and its synthetic applications in the field of nucleosides. Fil: Palacio, Cyntia M. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina Fil: Sabaini, María Belén. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina 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. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Article in Journal/Newspaper Antarc* Antarctica CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) Argentina Quilmes ENVELOPE(-55.617,-55.617,-63.233,-63.233) Journal of Biotechnology 165 2 99 101 |
| spellingShingle | Chemoselectivity Candida Antarctica Lipase B Acylase I Nucleobase N-Protection Oligonucleotide Building Blocks https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 Palacio, Cyntia M. Sabaini, María Belén Iribarren, Adolfo Marcelo Iglesias, Luis Emilio An efficient and mild access to N-acetyl protected purine nucleosides based on a chemoselective enzymatic hydrolysis |
| title | An efficient and mild access to N-acetyl protected purine nucleosides based on a chemoselective enzymatic hydrolysis |
| title_full | An efficient and mild access to N-acetyl protected purine nucleosides based on a chemoselective enzymatic hydrolysis |
| title_fullStr | An efficient and mild access to N-acetyl protected purine nucleosides based on a chemoselective enzymatic hydrolysis |
| title_full_unstemmed | An efficient and mild access to N-acetyl protected purine nucleosides based on a chemoselective enzymatic hydrolysis |
| title_short | An efficient and mild access to N-acetyl protected purine nucleosides based on a chemoselective enzymatic hydrolysis |
| title_sort | efficient and mild access to n-acetyl protected purine nucleosides based on a chemoselective enzymatic hydrolysis |
| topic | Chemoselectivity Candida Antarctica Lipase B Acylase I Nucleobase N-Protection Oligonucleotide Building Blocks https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 |
| topic_facet | Chemoselectivity Candida Antarctica Lipase B Acylase I Nucleobase N-Protection Oligonucleotide Building Blocks https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 |
| url | http://hdl.handle.net/11336/24092 |