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Glucosidase inhibitors block enzymes that cleave glucose units from oligosaccharides, disaccharides and glycoproteins. Intestinal α-glucosidases break down dietary carbohydrates, so their inhibitors are used to study postprandial glucose uptake. Acarbose, a pseudo-oligosaccharide, and miglitol, an iminosugar, are standard inhibitors of these enzymes. In the endoplasmic reticulum, glucosidases I and II trim glucose residues from newly attached N-linked glycans. Trimming and later reglucosylation control glycoprotein binding to the chaperone calnexin, as reported in 1995. Deoxynojirimycin and celgosivir inhibit these processing glucosidases and are used in glycoprotein folding and virology research. Miglustat hydrochloride, an N-alkylated iminosugar, also inhibits glucosylceramide synthase in glycosphingolipid research.
N-4′-(p-Trifluoromethylphenyl)butyl-DAB is a potent agonist of lysosomal acid α-glucosidase (GAA). This compound enhances intracellular GAA activity in a dose-dependent manner, specifically in fibroblasts from Pompe disease patients harboring the M519V mutation. It serves as a valuable tool for research into enzyme replacement therapies and the cellular mechanisms underlying lysosomal storage disorders.
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