112684-57-8

Upstream product

• 257602-61-2 Thiocarbonic acid O-phenyl ester O-((1R,2R,3R,4S)-2,3,4-tris-benzyloxy-5-benzyloxyimino-1-benzyloxymethyl-pentyl) ester 
• 4291-69-4 2,3,4,6-Tetra-O-benzyl-D-glucopyranose 
• 2687-43-6 O-benzylhydoxylamine hydrochloride 
• 112684-46-5 (E)-(2S,3R,4R,5R)-2,3,4,6-tetrakis-benzyloxy-5-hydroxyhexanal O-benzyloxime 
• 622-33-3 N-benzyloxyamine 
• 112684-52-3 thiocarbonic acid O-phenyl ester O-(2,3,4-tris-benzyloxy-5-benzyloxyimino-1-benzyloxymethyl-pentyl) ester 

Downstream Products

• 257602-65-6 N-((1R,2S,3S,4R,5R)-2,3,4-Tris-benzyloxy-5-benzyloxymethyl-cyclopentyl)-acetamide 

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.

Synthesis and evaluation of aminocyclopentitol inhibitors of β-glucosidases

(matrix presented) (1R,2S,3S,4R,5R)-4-Amino-5-(hydroxymethyl)cyclopentane-1,2,3-triol 1, prepared from D-glucose, inhibits β-glucosidases from Caldocellum saccharolyticum (Ki = 1.8 x 10-7 M) and from almonds (Ki = 3.4 x 10