 The study focused on synthesizing and testing the inhibition potential of one, four iminolixitols, and their ineralalkyl derivatives against four different GH38 alpha monosidases. The results showed that 6-deoxydim was the most potent inhibitor of Amantu with a key value of 0.19m. This compound also had similar selectivity profiles compared to DIM, which is a known inhibitor of GMAi. However, an ineralalkylation of 6-deoxydim resulted in a decrease in its potency, but an increase in its selectivity. Molecular modeling revealed that the structural and physical chemical properties of the inhibitor, enzyme complexes, were similar. This article was authored by Martin Kallnick, Serge Sestak, Eurykona, and others.