112684-46-5

Upstream product

• 4291-69-4 2,3,4,6-Tetra-O-benzyl-D-glucopyranose 
• 622-33-3 N-benzyloxyamine 
• 2687-43-6 O-benzylhydoxylamine hydrochloride 

Downstream Products

• 112684-52-3 thiocarbonic acid O-phenyl ester O-(2,3,4-tris-benzyloxy-5-benzyloxyimino-1-benzyloxymethyl-pentyl) ester 
• 112924-70-6 O-benzyl-N-[(1R,2S,3S,4R,5S)-2,3,4-tris-benzyloxy-5-benzyloxymethylcyclopentyl]-N-hydroxylamine 
• 112684-57-8 O-benzyl-N-[(1R,2S,3S,4R,5R)-2,3,4-tris-benzyloxy-5-benzyloxymethylcyclopentyl]-N-hydroxylamine 
• 257602-65-6 N-((1R,2S,3S,4R,5R)-2,3,4-Tris-benzyloxy-5-benzyloxymethyl-cyclopentyl)-acetamide 
• 257602-64-5 N-((1R,2S,3S,4R,5S)-2,3,4-Tris-benzyloxy-5-benzyloxymethyl-cyclopentyl)-acetamide 

Relevant academic research and scientific papers

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

Stereocontrolled Debenzylative Cycloetherification Reaction as a Route to Enantiopure C-Furanosides with Amino Substituents in the Side Chain

A highly efficient methodology of the preparation of synthetically important tetrahydrofuran derivatives with an amino substituent in the side chain is reported. This process is based on the stereocontrolled debenzylative cycloetherification (DBCE) reaction applied for chirons from the d-gluco-and d-manno-series and provides derivatives with new stereogenic centers. The influence of the electron-withdrawing group (EWG), present in the acyclic substrates with the mesyl leaving group, on the reactivity in the DBCE reaction was investigated both in the flask and by density functional theory (DFT) calculations. It was demonstrated that tetrahydrofuran derivatives with the benzoxime group (EWG = CHNOBn) are very good candidates for the subsequent highly stereoselective Grignard reaction.

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.