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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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_01681656_v165_n2_p99_Palacio |
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todo:paper_01681656_v165_n2_p99_Palacio2023-10-03T15:06:06Z 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. Acylase I Candida antarctica lipase B Chemoselectivity Nucleobase N-protection Oligonucleotide building blocks Acylase I Building blockes Candida antarctica lipase B 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 Hydrolysis Lipase Purine Nucleosides Aspergillus melleus Candida antarctica 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_01681656_v165_n2_p99_Palacio |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
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R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Acylase I Candida antarctica lipase B Chemoselectivity Nucleobase N-protection Oligonucleotide building blocks Acylase I Building blockes Candida antarctica lipase B 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 Hydrolysis Lipase Purine Nucleosides Aspergillus melleus Candida antarctica |
| spellingShingle |
Acylase I Candida antarctica lipase B Chemoselectivity Nucleobase N-protection Oligonucleotide building blocks Acylase I Building blockes Candida antarctica lipase B 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 Hydrolysis Lipase Purine Nucleosides Aspergillus melleus 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 Acylase I Building blockes Candida antarctica lipase B 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 Hydrolysis Lipase Purine Nucleosides Aspergillus melleus 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 |
JOUR |
| 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 |
http://hdl.handle.net/20.500.12110/paper_01681656_v165_n2_p99_Palacio |
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