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...
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ftunibueairesbd:todo:paper_01681656_v165_n2_p99_Palacio 2023-10-29T02:30:58+01:00 An efficient and mild access to N-acetyl protected purine nucleosides based on a chemoselective enzymatic hydrolysis Palacio, C.M. Sabaini, M.B. Iribarren, A.M. Iglesias, L.E. https://hdl.handle.net/20.500.12110/paper_01681656_v165_n2_p99_Palacio unknown http://hdl.handle.net/20.500.12110/paper_01681656_v165_n2_p99_Palacio info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar Acylase I Candida antarctica lipase B Chemoselectivity Nucleobase N-protection Oligonucleotide building blocks Building blockes Chemo-selectivity Nucleobases Enzymatic hydrolysis Isomers Oligonucleotides Biomolecules aminoacylase hydrolase purine nucleoside article Aspergillus melleus chemical reaction chemoselective enzymatic hydrolysis deacetylation deprotection reaction enzyme synthesis hydrolysis priority journal quantitative analysis synthesis Amidohydrolases Aspergillus Fungal Proteins Lipase Purine Nucleosides Candida antarctica JOUR ftunibueairesbd https://doi.org/20.500.12110/paper_01681656_v165_n2_p99_Palacio 2023-10-05T01:28:47Z 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. © 2013 Elsevier B.V. Journal/Newspaper Antarc* Antarctica Biblioteca Digital FCEN-UBA (Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires) |
institution |
Open Polar |
collection |
Biblioteca Digital FCEN-UBA (Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires) |
op_collection_id |
ftunibueairesbd |
language |
unknown |
topic |
Acylase I Candida antarctica lipase B Chemoselectivity Nucleobase N-protection Oligonucleotide building blocks Building blockes Chemo-selectivity Nucleobases Enzymatic hydrolysis Isomers Oligonucleotides Biomolecules aminoacylase hydrolase purine nucleoside article Aspergillus melleus chemical reaction chemoselective enzymatic hydrolysis deacetylation deprotection reaction enzyme synthesis hydrolysis priority journal quantitative analysis synthesis Amidohydrolases Aspergillus Fungal Proteins Lipase Purine Nucleosides Candida antarctica |
spellingShingle |
Acylase I Candida antarctica lipase B Chemoselectivity Nucleobase N-protection Oligonucleotide building blocks Building blockes Chemo-selectivity Nucleobases Enzymatic hydrolysis Isomers Oligonucleotides Biomolecules aminoacylase hydrolase purine nucleoside article Aspergillus melleus chemical reaction chemoselective enzymatic hydrolysis deacetylation deprotection reaction enzyme synthesis hydrolysis priority journal quantitative analysis synthesis Amidohydrolases Aspergillus Fungal Proteins Lipase Purine Nucleosides Candida antarctica Palacio, C.M. Sabaini, M.B. Iribarren, A.M. Iglesias, L.E. An efficient and mild access to N-acetyl protected purine nucleosides based on a chemoselective enzymatic hydrolysis |
topic_facet |
Acylase I Candida antarctica lipase B Chemoselectivity Nucleobase N-protection Oligonucleotide building blocks Building blockes Chemo-selectivity Nucleobases Enzymatic hydrolysis Isomers Oligonucleotides Biomolecules aminoacylase hydrolase purine nucleoside article Aspergillus melleus chemical reaction chemoselective enzymatic hydrolysis deacetylation deprotection reaction enzyme synthesis hydrolysis priority journal quantitative analysis synthesis Amidohydrolases Aspergillus Fungal Proteins Lipase Purine Nucleosides Candida antarctica |
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. © 2013 Elsevier B.V. |
format |
Journal/Newspaper |
author |
Palacio, C.M. Sabaini, M.B. Iribarren, A.M. Iglesias, L.E. |
author_facet |
Palacio, C.M. Sabaini, M.B. Iribarren, A.M. Iglesias, L.E. |
author_sort |
Palacio, C.M. |
title |
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_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_sort |
efficient and mild access to n-acetyl protected purine nucleosides based on a chemoselective enzymatic hydrolysis |
url |
https://hdl.handle.net/20.500.12110/paper_01681656_v165_n2_p99_Palacio |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
http://hdl.handle.net/20.500.12110/paper_01681656_v165_n2_p99_Palacio |
op_rights |
info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar |
op_doi |
https://doi.org/20.500.12110/paper_01681656_v165_n2_p99_Palacio |
_version_ |
1781064225876082688 |