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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Main Authors:	Palacio, C.M., Sabaini, M.B., Iribarren, A.M., Iglesias, L.E.
Format:	Journal/Newspaper
Language:	unknown
Subjects:	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 Antarc* Antarctica
Online Access:	https://hdl.handle.net/20.500.12110/paper_01681656_v165_n2_p99_Palacio

id	ftunibueairesbd:todo:paper_01681656_v165_n2_p99_Palacio
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spelling	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

An efficient and mild access to N-acetyl protected purine nucleosides based on a chemoselective enzymatic hydrolysis

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