134308-87-5

Upstream product

• 1676-81-9 N-benzyloxycarbonyl-L-serine methyl ester 
• 501-53-1 benzyl chloroformate 
• 55692-87-0 isopropyl 2,3,4,6-tetra-O-acetyl-1-thio-β-D-galactopyranoside 
• 367-93-1 isopropyl β-D-thiogalactopyranoside 
• 14364-68-2 O-(2,3,4,6-tetra-O-acetyl-β-D-galactopyranosyl)-N-benzyloxycarbonyl-L-serine methyl ester 
• 2280-44-6 D-Glucose 
• 1145-80-8 N-(benzyloxycarbonyl)-L-serine 

Downstream Products

• 440652-77-7 O-(2,3,4-tri-O-benzoyl-6-o-trityl-β-D-galactopyranosyl)-N-benzyloxycarbonyl-L-serine methyl ester 
• 440652-78-8 O-(2,3,4-tri-O-benzoyl-β-D-galactopyranosyl)-N-benzyloxycarbonyl-L-serine methyl ester 

Relevant academic research and scientific papers

Straightforward glycosylation of alcohols and amino acids mediated by ionic liquid

Green glycosylation of functionalized alcohols and α-amino acids, using an ionic liquid as a recyclable solvent, was performed in one step directly from the unprotected monosaccharide under scandium triflate or ferric chloride catalysis. Pure α- and β-glycosides could be obtained after specific enzymatic hydrolysis.

"Polar patch" proteases as glycopeptiligases

The strategy of combined site directed mutagenesis and chemical modification with polar prosthetic groups was used to broaden substrate specificity of proteases resulting in the first successful formation of glycopeptides through the use of glucoamino acid acyl donors in yields of up to 90%.

A simple access to 3,6-branched oligosaccharides: Synthesis of a glycopeptide derivative that relates to Lycium barbarum L.

An efficient method is described for the synthesis of galactopyranosyl-containing 3,6-branched oligosaccharides using isopropyl thiogalactopyranoside as starting material. This method is successfully applied to the preparation of a glycopeptide derivative that relates to Lycium barbarum L. The potential application of isopropyl thioglycoside in glycosylation is also investigated.

Synthesis of O-β-galactopyranosyl-L-serine derivatives using β-galactosidase in aqueous-organic reaction systems

The galactosylation of amino protected serine methyl ester derivatives by β -galactosidases from E. coli and A. oryzae in aqueous-organic solvents was investigated. A comparison of enzyme activity in aqueous buffer and in several aqueous-organic mixtures revealed that the presence of an organic solvent normally causes a loss in enzyme activity. When the enzyme is used in suspensions with mainly undissolved lactose, the detrimental influence of an organic solvent is less marked if it does not exceed 25 % of the added mixture with water. Employing organic cosolvents, such as acetonitrile, 2-butanone, acetone or ethyl acetate, we obtained yields of the desired galactosylation products higher than those with the enzyme in purely aqueous solution. The amino protecting group shows a significant influence on the transglycosylation reaction in terms of yield, the best up to 28 % being achieved in the synthesis of Aloc-(Ga1β1-)Ser-OMe with β-galactosidase from E. coli in a reaction mixture containing 8 to 15 % organic solvent.