An Enzymatic Flow-Based Preparative Route to Vidarabine

    • Lucia Tamborini1*
    • Clelia Previtali1
    • Francesca Annunziata1
    • Teodora Bavaro2
    • Marco Terreni2
    • Enrica Calleri2
    • Francesca Rinaldi2
    • Andrea Pinto3
    • Giovanna Speranza4
    • Daniela Ubiali2*
    • Paola Conti1
    • 1Department of Pharmaceutical Sciences, University of Milan, via Mangiagalli 25, 20133 Milano, Italy
    • 2Department of Drug Sciences, University of Pavia, viale Taramelli 12, 27100 Pavia, Italy
    • 3Department of Food, Environmental and Nutritional Sciences, University of Milan, via Celoria 2, 20133 Milano, Italy
    • 4Department of Chemistry, University of Milan, via Golgi 19, 20133 Milano, Italy

    The bi-enzymatic synthesis of the antiviral drug vidarabine (arabinosyladenine, ara-A), catalyzed by uridine phosphorylase from Clostridium perfringens (CpUP) and a purine nucleoside phosphorylase from Aeromonas hydrophila (AhPNP), was re-designed under continuous-flow conditions. Glyoxyl–agarose and EziGTM1 (Opal) were used as immobilization carriers for carrying out this preparative biotransformation. Upon setting-up reaction parameters (substrate concentration and molar ratio, temperature, pressure, residence time), 1 g of vidarabine was obtained in 55% isolated yield and >99% purity by simply running the flow reactor for 1 week and then collecting (by filtration) the nucleoside precipitated out of the exiting flow. Taking into account the substrate specificity of CpUP and AhPNP, the results obtained pave the way to the use of the CpUP/AhPNP-based bioreactor for the preparation of other purine nucleosides.

    Get in touch

    For more information on flow chemistry systems and services please use the contact methods below.

    Call us on +44 (0)1284 728659 or Email us

    Request a quote