Synthesis and glycosidase inhibitory activity of new hexa- substituted C8-glycomimetics

• Olivia Andriuzzi,
• Christine Gravier-Pelletier,
• Gildas Bertho,
• Thierry Prangé and
• Yves Le Merrer

Beilstein J. Org. Chem. 2005, 1, No. 12, doi:10.1186/1860-5397-1-12

• and human placenta, α-D-galactosidases from coffee beans and Escherichia coli, β-D-galactosidases from Escherichia coli, bovine liver, Aspergillus niger and Aspergillus orizae, α-N-acetylgalactosaminidase from chicken liver, β-N-acetylglucosaminidases from Jack bean, bovine epididymis A and bovine

• epididymis B, α-D-mannosidase from almonds, β-D-mannosidase from Helix pomatia, and β-xylosidase from Aspergillus niger. For other enzymes: α-D-glucosidase from Bacillus stearothermophilus, amyloglucosidase from Aspergillus niger and Rhizopus mold, β-D-glucosidase from almonds, α-L-fucosidase from bovine

• correlated with an increase in observed activity. Thus, for example we had previously shown that the corresponding C7-voglibose mimic exhibited interesting activity towards amyloglucosidases from Aspergillus niger and Rhizopus mold (35 and 18 μM respectively, unpublished results). Furthermore, even if data