65877-26-1

Upstream product

• 3162-96-7 methyl-4,6-O-phenylmethylene-α-D-mannopyranoside 
• 65877-24-9 methyl 3-O-allyl-4,6-O-benzylidene-α-D-mannopyranoside 
• 65817-35-8 methyl 3-O-allyl-2-O-methyl-4,6-O-benzylidene-α-D-mannopyranoside 
• 120408-72-2 Methyl 2,3-anhydro-4,6-O-(phenylmethylene)-β-D-allopyranoside 
• 124-41-4 sodium methylate 
• 2880-96-8 methyl 2,3-anhydro-4,6-O-benzylidene-β-D-gulopyranoside 
• 86470-08-8 methyl 4,6-O-benzylidene-β-D-galactopyranoside 3-O-p-toluenesulfonate 
• 71117-36-7 methyl 4,6-O-(S)-benzylidene-β-D-galactopyranoside 
• 1824-94-8 methyl beta-D-galactopyranoside 

Downstream Products

• 3013-58-9 methyl 4,6-O-(S)-benzylidene-2,3-di-O-methyl-β-D-idopyranoside 

Relevant academic research and scientific papers

A scalable approach to obtaining orthogonally protected β-d-idopyranosides

A practical method to obtain orthogonally protected d-idopyranose from d-galactose has been developed, which is the first method to enable synthesis of the challenging β-d-idopyranoside linkage. The method relies on a key double inversion at O-2 and O-3 in an easily prepared d-galactose derivative, which proceeds regio- and stereoselectively through a 2,3-anhydrotalopyranoside; reaction using a selection of alkoxides affords exclusively the 3-O-alkylidopyranoside, which can be used to generate an orthogonally protected monosaccharide. The process is scalable and requires minimal purification, so it could be used to produce building blocks to aid in the synthesis of various β-idopyranose-containing oligosaccharide targets to further probe their biological functions.

Analysis of the binding specificities of oligomannoside-binding proteins using methylated monosaccharides

The binding specificities of the closely related lectins from Canavalia ensiformis and Dioclea grandiflora were examined using specifically O-alkylated mono- and disaccharides. Both lectins accept any substitution at the monosaccharide C2 hydroxyl group. The binding energy of C2-alkylated ligands-concanavalin A complexes increases by 1 kcal mol-1 for the C2-O-ethyl ligand, while the binding energies of the corresponding complexes with the Dioclea lectin are identical. Both lectins accept methyl, but not ethyl, substitution of the C3 hydroxyl, in contrast to earlier reports. The results are interpreted in terms of existing models of the concanavalin A binding site. While the results are consistent with a model of the concanavalin A extended binding site that places the non-reducing terminus of all disaccharides in the monosaccharide binding site, they point to the dangers of interpreting the binding behavior of unnatural saccharide ligands on the basis of crystallographic data obtained with native ligands.