196097-71-9

Upstream product

• 73724-48-8 N-(fluoren-9-ylmethoxycarbonyl)-L-threonine benzyl ester 
• 144923-59-1 ethyl 3,4,6-tri-O-acetyl-2-deoxy-1-thio-2-(2,2,2-trichloroethoxycarbonylamino)-β-D-glucopyranoside 
• 172490-46-9 2-deoxy-2-(2,2,2-trichloroethoxycarbonylamino)-D-glucopyranose 
• 136945-14-7 O-[3,4,6-tri-O-acetyl-2-deoxy-2-(2,2,2-trichloroethoxycarbonylamino)-α-D-glucopyranosyl] trichloroacetimidate 
• 136945-13-6 [(2R,3S,4R,5R)-3,4-diacetoxy-6-hydroxy-5-(2,2,2-trichloroethoxycarbonylamino)tetrahydropyran-2-yl]methyl acetate 
• 122210-01-9 1,3,4,6-tetra-O-acetyl-2-deoxy-2-(2,2,2-trichloroethoxycarbonylamino)-D-glucopyranose 
• 1078691-95-8 (+)-D-glucosamine hydrochloride 
• 122210-05-3 1,3,4,6-tetra-O-acetyl-2-deoxy-2-(2,2,2-trichloroethoxycarbonylamino)-β-D-glucopyranose 
• 5432-46-2 1,3,4,6-tetra-O-acetyl-D-glucosamine hydrochloride 
• 51471-40-0 Anisalglucosamin 
• 14257-69-3 glucosamine 

Downstream Products

• 196313-91-4 N^α-fluoren-9-ylmethoxycarbonyl-O-(2-acetamido-2-deoxy-3,4,6-tri-O-acetyl-β-D-glucopyranosyl)-L-threonine benzylester 

Relevant academic research and scientific papers

Glycosylation of threonine of the repeating unit of RNA polymerase II with β-linked N-acetylglucosame leads to a turnlike structure

Two models of the repeating C-terminal domain of RNA polymerase II (Ac- SYSPTSPSYS-NH2; Ac-SYSPT(β-O-GlcNAc)SPSYS-NH2) were prepared and their conformations in water studied using 1-D and 2-D 1H NMR spectroscopies, CD spec

Glycosylated analogs of formaecin I and drosocin exhibit differential pattern of antibacterial activity

The synthetic glycopeptides are interesting model systems to study the effect of O-glycosylation in modulating their function and structure. A series of glycosylated analogs of two antibacterial peptides, formaecin I and drosocin, were synthesized by varying the nature of sugar and its linkage with bioactive peptides to understand the influence of structure variation of glycosylation on their antibacterial activities. Higher antibacterial activities of all glycopeptides compared to their respective non-glycosylated counterparts emphasize in part the importance of sugar moieties in functional implications of these peptides. The consequences of the unique differences among the analogs were apparent on their antibacterial activities but not evident structurally by circular dichroism studies. We have shown that differently glycosylated peptides exhibit differential effect among each other when tested against several Gram-negative bacterial strains. The change of monosaccharide moiety and/or its anomeric configuration in formaecin I and drosocin resulted into decrease in the antibacterial activity in comparison to that of the native glycopeptide, but the extent of decrease in antibacterial activity of glycosylated drosocin analogs was less. Probably, the variation in peptide conformation arising due to topological dissimilarities among different sugars in the same peptide resulting in possible modulation in binding properties appears to be responsible for differences in their antibacterial activities. Indeed, these effects of glycosylation are found to be sequence-specific and depend in the milieu of amino acid residues. Interestingly, none of the carbohydrate variants affected the basic property of these peptides, which is non-hemolytic and non-toxicity to eukaryotic cells. The Author(s) 2011.

Chemoenzymatic solution- and solid-phase synthesis of O-glycopeptides of the mucin domain of MAdCAM-1. A general route to O-LacNAc, O-sialyl-LacNAc, and O-Sialyl-Lewis-X peptides

An efficient and general method for the solid-phase synthesis of glycopeptides containing an O-linked sialyl-Lewis-X (SLe(x)) tetrasaccharide is described. Using a combined chemoenzymatic approach, the first synthesis of an unnatural β-O-linked SLe(x) att