Issue 13, 2009

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

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

Article information

Article type
Paper
Submitted
06 Apr 2009
Accepted
09 Apr 2009
First published
22 May 2009

Org. Biomol. Chem., 2009,7, 2738-2747

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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