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Issue 9, 2016
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Understanding multivalent effects in glycosidase inhibition using C-glycoside click clusters as molecular probes

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Abstract

The synthesis of the first examples of multivalent C-glycosides based on C60-fullerene or β-cyclodextrin cores by way of Cu(I)-catalyzed azide–alkyne cycloadditions is reported. These compounds were designed as molecular probes to understand the mechanisms underlying the outstanding multivalent effects observed in glycosidase inhibition. The inhibition results obtained support a multivalent-binding model based on two scenarios both involving nonspecific interactions and varying by the presence or the absence of active site specific interactions. The magnitude of the multivalent effect obtained depends on the identity of the glycosidase involved and more specifically on the accessibility of its catalytic active site. Large inhibitory multivalent effects can be obtained when both glycosidase active sites and non-catalytic sites at the protein surface are involved in binding events. On the other hand, nonspecific interactions alone are not sufficient to achieve relative affinity enhancements exceeding a simple statistical effect (i.e., a relative inhibition potency not better than one on a valence-corrected basis).

Graphical abstract: Understanding multivalent effects in glycosidase inhibition using C-glycoside click clusters as molecular probes

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Supplementary files

Article information


Submitted
25 Apr 2016
Accepted
09 Jun 2016
First published
10 Jun 2016

This article is Open Access

New J. Chem., 2016,40, 7421-7430
Article type
Paper

Understanding multivalent effects in glycosidase inhibition using C-glycoside click clusters as molecular probes

F. Stauffert, A. Bodlenner, T. M. Nguyet Trinh, M. I. García-Moreno, C. Ortiz Mellet, J. Nierengarten and P. Compain, New J. Chem., 2016, 40, 7421
DOI: 10.1039/C6NJ01311B

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