665019-69-2

Upstream product

• 665019-68-1 methyl 2-acetamido-6-azido-3-O-benzyl-2,6-dideoxy-4-O-(2-O-acetyl-3,4,6-tri-O-benzyl-β-D-galactopyranosyl)-β-D-glucopyranoside 
• 440345-39-1 methyl 2-acetamido-2-deoxy-3-O-benzyl-6-O-tert-butyldimethylsilyl-4-O-(2-O-acetyl-3,4,6-tri-O-benzyl-β-D-galactopyranosyl)-β-D-glucopyranoside 
• 440345-42-6 methyl 2-acetamido-2-deoxy-3-O-benzyl-6-O-methanesulfonyl-4-O-(2-O-acetyl-3,4,6-tri-O-benzyl-β-D-galactopyranosyl)-β-D-glucopyranoside 
• 440345-40-4 methyl 2-acetamido-2-deoxy-3-O-benzyl-4-O-(2-O-acetyl-3,4,6-tri-O-benzyl-β-D-galactopyranosyl)-β-D-glucopyranoside 

Downstream Products

• 665019-70-5 methyl 2-acetamido-6-amino-3-O-benzyl-2,6-dideoxy-4-O-(3,4,6-tri-O-benzyl-β-D-galactopyranosyl)-β-D-glucopyranoside 
• 704907-13-1 N-[(2R,3R,4R,5R,6R)-6-Azidomethyl-4-benzyloxy-5-((2S,3R,4S,5S,6R)-4,5-bis-benzyloxy-6-benzyloxymethyl-3-methoxy-tetrahydro-pyran-2-yloxy)-2-methoxy-tetrahydro-pyran-3-yl]-acetamide 
• 665019-72-7 methyl 2-acetamido-3-O-benzyl-2,6-dideoxy-2',6-(2'-O-methylenelactam)-4-O-(3,4,6-tri-O-benzyl-β-D-galactopyranosyl)-β-D-glucopyranoside 
• 665019-71-6 methyl 2-acetamido-3-O-benzyl-6-chloroacetamido-2,6-dideoxy-4-O-(3,4,6-tri-O-benzyl-β-D-galactopyranosyl)-β-D-glucopyranoside 

Relevant academic research and scientific papers

Glycosyltransferase activity can be selectively modulated by chemical modifications of acceptor substrates

A range of N-acetyllactosamine derivatives, which are modified by a wide range of functionalities at C-2′ and C-6, have been synthesised and the kinetic parameters of transfer catalysed by recombinant α-2,6-sialyltransferase and α-1,3-fucoyltra

Chemo-enzymatic synthesis of conformationally constrained oligosaccharides.

N-Acetyllactosamine derivative 4, which has a methylene amide tether between C-6 and C-2', was enzymatically glycosylated using rat liver alpha-2,6-sialyltransferase (ST6GalI) or recombinant human fucosyltransferase V (FucT-V) to give conformationally constrained trisaccharides 5 and 6, respectively. The methylene amide linker of 4 was installed by a two-step procedure, which involved acylation of a C-6 amino function of a LacNAc derivative with chloroacetic anhydride followed by macrocyclization by nucleophilic displacement of the chloride by a C-2' hydroxyl. The conformational properties of 4 were determined by a combination of NOE and trans-glycosidic heteronuclear coupling constant measurements and molecular mechanics simulations and these studies established that the glycosidic linkage of 4 is conformationally constrained and resides in only one of the several energy minima accessible to LacNAc. The apparent kinetic parameters of transfer to LacNAc and conformationally constrained saccharides 3 and 4 indicates that fucosyltransferase V recognize LacNAc in its A-conformer whereas alpha-2,6-sialyltransferase recognizes the B-conformer of LacNAc.