Fiaux, HélèneKuntz, Douglas A.Janzer, Robert C.Gerber-Lemaire, SandrineRose, David R.Juillerat-Jeanneret, Lucienne2008-06-052008-06-052008-06-05200810.1016/j.bmc.2008.06.021https://infoscience.epfl.ch/handle/20.500.14299/26123WOS:000258749500028Refining the chemical structure of functionalized pyrrolidine-based inhibitors of Golgi α- mannosidase II (GMII) to optimize binding affinity provided a lead molecule that demonstrated nanomolar competitive inhibition of α-mannosidases II and an optimal fit in the active site of Drosophila GMII by X-ray crystallography. Esters of this lead compound also inhibited the growth of human glioblastoma and brain-derived endothelial cells more than the growth of non-tumoral human fibroblasts, suggesting their potential for anti-cancer therapy.alpha-mannosidase inhibitorsX-ray crystallographyglioblastomaanti-cancer agentstext::journal::journal article::research article