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

• 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

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.