We here report on the enzymatic synthesis of the antiviral drug vidarabine (arabinosyladenine, araA) starting from arabinosyluracil and adenine. To this aim, uridine phosphorylase from Clostridium perfringens (CpUP) and a purine nucleoside phosphorylase from Aeromonas hydrophila (AhPNP) were used as covalently immobilized biocatalysts. Upon investigation of the optimal conditions for the enzyme activity (phosphate buffer 25 mM, pH 7.5, 25 °C, DMF 12.5-30%), the synthesis of araA was scaled up (2 L) and the product was isolated in 53% yield (3.5 g L-1) and 98.7% purity. An E-factor comparison between the enzymatic synthesis of araA and the classical chemical procedure clearly highlighted the "greenness" of the enzymatic route over the chemical one (E-factor: 423 vs. 1356, respectively). copy; The Royal Society of Chemistry 2015.

Serra, I., Daly, S., Alcantara, A., Bianchi, D., Terreni, M., Ubiali, D. (2015). Redesigning the synthesis of vidarabine via a multienzymatic reaction catalyzed by immobilized nucleoside phosphorylases. RSC ADVANCES, 5(30), 23569-23577 [10.1039/c4ra15018j].

Redesigning the synthesis of vidarabine via a multienzymatic reaction catalyzed by immobilized nucleoside phosphorylases

Serra I.
;
2015

Abstract

We here report on the enzymatic synthesis of the antiviral drug vidarabine (arabinosyladenine, araA) starting from arabinosyluracil and adenine. To this aim, uridine phosphorylase from Clostridium perfringens (CpUP) and a purine nucleoside phosphorylase from Aeromonas hydrophila (AhPNP) were used as covalently immobilized biocatalysts. Upon investigation of the optimal conditions for the enzyme activity (phosphate buffer 25 mM, pH 7.5, 25 °C, DMF 12.5-30%), the synthesis of araA was scaled up (2 L) and the product was isolated in 53% yield (3.5 g L-1) and 98.7% purity. An E-factor comparison between the enzymatic synthesis of araA and the classical chemical procedure clearly highlighted the "greenness" of the enzymatic route over the chemical one (E-factor: 423 vs. 1356, respectively). copy; The Royal Society of Chemistry 2015.
Articolo in rivista - Articolo scientifico
vidarabine; nucleoside phosphorylase; biocatalysis;
English
2015
5
30
23569
23577
none
Serra, I., Daly, S., Alcantara, A., Bianchi, D., Terreni, M., Ubiali, D. (2015). Redesigning the synthesis of vidarabine via a multienzymatic reaction catalyzed by immobilized nucleoside phosphorylases. RSC ADVANCES, 5(30), 23569-23577 [10.1039/c4ra15018j].
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/316402
Citazioni
  • Scopus 30
  • ???jsp.display-item.citation.isi??? 28
Social impact