Glycosidase inhibition by ring-modified castanospermine analogues: tackling enzyme selectivity by inhibitor tailoring
Organic & Biomolecular Chemistry2009Vol. 7(13), pp. 2738–2738
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Matilde Aguilar‐Moncayo, T.M. Gloster, J.P. Turkenburg, M. Isabel García‐Moreno, Carmen Ortiz Mellet, G.J. Davies, José M. Garcı́a Fernández
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 beta-glucosidase inhibitors with unusual binding signatures; the presence of an N-octyl substituent imparts a remarkable anomeric selectivity, promoting strong binding of the appropriate beta-anomer by the beta-glucosidase.
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