New findings on biological activity of iminosugars

CARB 32

Naoki Asano, naoki22@po.incl.ne.jp, Faculty of Pharmaceutical Sciences, Hokuriku University, Ho-3 Kanagawa-machi, Kanazawa, 920-1181, Japan
D-Iminosugars are competitive inhibitors of D-glycosidases, whereas their L-enantiomers were noncompetitive inhibitors of the enzymes. 1,4-Dideoxy-1,4-imino-L-arabinitol (L-AB1) and 2,5-dideoxy-2,5-imino-L-mannitol (L-DMDP) are very potent noncompetitive inhibitors of isomaltase with Ki values of 0.07 and 0.023 μM, respectively. D-AB1 and D-isofagomine are potent inhibitors of glycogen phosphorylase b. The multiple inhibition analysis by two inhibitors showed that D-AB1 and D-isofagomine do not bind the catalytic site but bind both of the AMP activatory and the caffeine-binding sites. The addition of subinhibitory concentrations of N-nonyl-D-1-deoxynojirimycin (N-nonyl-D-DNJ) and α-1-C-octyl-D-DNJ to culture medium for 10 days led to 2.3- and 1.9-fold increases in the β-glucosidase activity of the fibroblasts derived from N370S Gaucher patients. Although the addition of α-1-C-octyl-D-DNJ gave no effect on a lysosomal α-glucosidase activity, that of N-nonyl-D-DNJ caused 50% inhibition of the activity throughout 10 days.
 

Iminosugars: Therapeutic Potential
8:30 AM-12:10 PM, Tuesday, 30 August 2005 Washington DC Convention Center -- 202A, Oral

Division of Carbohydrate Chemistry

The 230th ACS National Meeting, in Washington, DC, Aug 28-Sept 1, 2005