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Issue 13, 2009
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Glycosidase inhibition by ring-modified castanospermine analogues: tackling enzyme selectivity by inhibitor tailoring

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Abstract

Synthesis of a panel of iso(thio)urea-type ring-modified castanospermine analogues bearing a freely mutarotating pseudoanomeric hydroxyl group results in tight-binding β-glucosidase inhibitors with unusual binding signatures; the presence of an N-octyl substituent imparts a remarkable anomeric selectivity, promoting strong binding of the appropriate β-anomer by the β-glucosidase.

Graphical abstract: Glycosidase inhibition by ring-modified castanospermine analogues: tackling enzyme selectivity by inhibitor tailoring

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Publication details

The article was received on 06 Apr 2009, accepted on 09 Apr 2009 and first published on 22 May 2009


Article type: Paper
DOI: 10.1039/B906968B
Citation: Org. Biomol. Chem., 2009,7, 2738-2747
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    Glycosidase inhibition by ring-modified castanospermine analogues: tackling enzyme selectivity by inhibitor tailoring

    M. Aguilar-Moncayo, T. M. Gloster, J. P. Turkenburg, M. I. García-Moreno, C. Ortiz Mellet, G. J. Davies and J. M. García Fernández, Org. Biomol. Chem., 2009, 7, 2738
    DOI: 10.1039/B906968B

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