Système touristique et culture technique dans l'Arc lémanique : analyse d'une success story et de ses effets sur l'économie régionale (1852-1914)

Inhibition of glycosidases has great potential in the quest for highly potent and specific drugs to treat diseases such as diabetes, cancer, and viral infections. One of the most effective ways of designing such compounds is by mimicking the transition state. Here we describe the structural, kinetic, and thermodynamic dissection of binding of two glucoimidazole-derived compounds, which are among the most potent glycosidase inhibitors reported to date, with two family 1 beta-glycosidases. Provocatively, while inclusion of the phenethyl moiety improves binding by a factor of 20-80-fold, this does not appear to result from better noncovalent interactions with the enzyme; instead, improved affinity may be derived from significantly better entropic contributions to binding displayed by the phenethyl-substituted imidazole compound

Glycosidase inhibition: assessing mimicry of the transition state

A review of the progress made in tackling glycosidase inhibition, which has widespread application in a number of diseases, in particular by examining those inhibitors that may mimic the transition state