732308-55-3

Upstream product

• 732308-53-1 (1R,2R,3R,4S)-1-bromo-3,4-O-isopropylidene-5-methylenecyclopentane-2,3,4-triol 
• 247191-05-5 (2S,3S,4S,5R)-1-methylene-2,3-O-isopropylidene-2,3-dihydroxy-4,5-epoxycyclopentane 
• 732308-48-4 (3aR,6S,6aS)-6-methoxy-2,2-dimethyldihydrofuro[3,4-d][1,3]dioxol-4(3aH)-one 
• 247191-04-4 (2R,3R,4S,5R)-2,3-O-isopropylidene-2,3-dihydroxy-4,5-epoxycyclopentanone 
• 115509-13-2 (3aR,6aR)-2,2-Dimethyl-3a,6a-dihydro-cyclopenta[1,3]dioxol-4-one 
• 63029-07-2 methyl 2,3-O-isopropylidene-α-D-lyxofuranoside 
• 4099-88-1 (3aS,6R,6aS)-6-(hydroxymethyl)-2,2-dimethyl-tetrahydrofuro[3,4-d]-[1,3]dioxol-4-ol 
• 732308-54-2 (1R,2R,3S,4S)-1-bromo-2-O-(N-benzylcarbamoyl)-3,4-O-isopropylidene-5-methylenecyclopentane-2,3,4-triol 

Downstream Products

• 732308-57-5 (1S,2S,3S,4S,5R)-4-benzylamino-3-O-4-N-(oxomethylidene)-1,2-O-isopropylidene-5-((tert-butyl-dimethylsilyloxy)methyl)cyclopentane-1,2,3-triol 
• 732308-58-6 (1S,2S,3S,4S,5R)-4-benzylamino-5-(hydroxymethyl)-1,2-isopropylidenecyclopentane-1,2,3-triol 
• 732308-42-8 (1S,2S,3S,4S,5R)-4-N-benzylamino-5-hydroxymethyl-cyclopentane-1,2,3-triol 
• 732308-56-4 (1R,2R,3S,4S,5R)-2-O-(N-benzylcarbamoyl)-1-bromo-5-(O-tert-butyldimethylsilyloxymethyl)-3,4-O-isopropylidenecyclopentane-1,2,3-triol 

Relevant academic research and scientific papers

Structure-activity relationships in aminocyclopentitol glycosidase inhibitors

Aminocyclopentitol analogs of β-D-glucose, β-D-galactose and α-D-galactose bearing alkyl substituents as aglycon mimics on the amine function were prepared and tested for inhibition of various glycosidases. N-benzyl-β-D-gluco derivatives 1-4 and N-benzyl-β-D-galacto derivative 5 inhibited β-galactosidase and β-glucosidase. N-benzyl-α-D- galacto aminocyclopentitol 6 strongly inhibited α-galactosidase. The inhibitory activities observed were generally stronger compared to those of their primary amine analogs. A structure-activity relationship analysis was carried out including data from thirty-five different aminocyclopentitol glycosidase inhibitors. The strongest inhibitions reported for any enzyme were associated with a perfect stereochemical match between aminocyclopentitol and glycosidase, including the α- or β-configuration of the amino-group corresponding to the enzyme's anomeric selectivity.