Monomeric and dimeric benzylated glycosyl benzenes were synthesized via copper-catalyzed [3 + 2] azide-alkyne cycloaddition These compounds were then identified as protein tyrosine phosphatase (PTP) 1B inhibitors which displayed at least several fold selectivity over other homologous PTPases The glucosyl, galactosyl, and mannosyl inhibitors exhibited different biological profiles, suggesting the monosaccharides may qualify as chiral scaffolds for probing the spatial preference of PTP1B Furthermore, docking study suggested a plausible binding mode of this glycoside series with the enzymatic target