28619-28-5

Upstream product

• 530-26-7 D-Mannose 
• 83-87-4 D-Mannose pentaacetate 
• 106-41-2 4-bromo-phenol 
• 4163-65-9 per-O-acetyl-α-D-mannopyranose 
• 121238-27-5 2,3,4,6-tetra-O-acetyl-α-D-mannopyranosyl trichloroimidate 

Downstream Products

• 1259428-41-5 methyl 4'-(2,3,4,6-tetra-O-acetyl-α-D-mannopyranosyloxy)-biphenyl-4-carboxylate 
• 1259474-47-9 4'-(α-D-mannopyranosyloxy)-biphenyl-4-carboxylic acid 
• 1295649-89-6 4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl 2,3,4,6-tetra-O-acetyl-α-D-mannopyranoside 
• 1295649-64-7 methyl 5-[4-(α-D-mannopyranosyloxy)phenyl]pyridine-3-carboxylate 
• 1231608-88-0 C₂₇H₂₇NO₁₀ 
• 1231608-13-1 3-[4-[(2R,3S,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)-tetrahydropyran-2-yl]oxyphenyl]benzonitrile 
• 28541-77-7 4-bromophenyl α-D-mannopyranoside 

Relevant academic research and scientific papers

Preparation and characterization of glycopolymers with biphenyl spacers: Via Suzuki coupling reaction

Poly(vinylbiphenyl)s bearing glycoside ligands at the side chains were prepared using the Suzuku coupling reaction. Effects of glycoside reactant concentration, halide species, glycoside species, and catalyst species on the incorporation of glycoside ligand into the polymer were investigated. The obtained glycopolymers exhibited specific binding to proteins corresponding to the glycoside ligands. In addition, the biphenyl spacers formed by the Suzuki coupling reaction in the glycopolymer were fluorescent, whereas the polymer precursor was not.

Bifunctional mannoside-glucosinolate glycoconjugates as enzymatically triggered isothiocyanates and FimH ligands

Glucosinolates are sulfur-containing secondary metabolites found in plants of the Brassicale order. They are precursors of isothiocyanate species, resulting from C-S hydrolysis catalysed by the thioglucohydrolase myrosinase. We describe the synthesis of bifunctional glucosinolate-mannoside glycoconjugates combining both the structural features of a substrate of myrosinase and a ligand of the lectin FimH. We show that these glycoconjugates serve as enzyme substrates and that myrosinase can indeed hydrolyze the glucosinolate moiety with affinities (KM, Vmax) comparable to the natural substrates glucomoringin and sinigrin. This enzymatic hydrolysis of the thioglycosidic bond led to the efficient formation of an isothiocyanate which was assessed by the formation of the corresponding dithiocarbamate derivatives. Finally, we show that our synthetic bifunctional glycoconjugates also serve as FimH ligands where the glucosinolate moiety does not hamper the interaction with the lectin. Our findings set the stage for an original bioconjugation tool, allowing for myrosinase-triggered specific labelling of lectins using glucosinolate glycoconjugates as non-toxic, water soluble isothiocyanate precursors.

MANNOSE DERIVATIVES AS ANTAGONISTS OF BACTERIAL ADHESION

Compounds of the formula (I) wherein n is 0, 1 or 2, R1 is aryl, heteroaryl or heterocyclyl, and R2 and R3 are hydrogen or a substituent as described in the specification, are useful for the prevention and treatment of bacterial infections, in particular of urinary infections caused by E. coli.

FimH antagonists for the oral treatment of urinary tract infections: From design and synthesis to in vitro and in vivo evaluation

Urinary tract infection (UTI) by uropathogenic Escherichia coli (UPEC) is one of the most common infections, particularly affecting women. The interaction of FimH, a lectin located at the tip of bacterial pili, with high mannose structures is critical for the ability of UPEC to colonize and invade the bladder epithelium. We describe the synthesis and the in vitro/in vivo evaluation of α-d-mannosides with the ability to block the bacteria/host cell interaction. According to the pharmacokinetic properties, a prodrug approach for their evaluation in the UTI mouse model was explored. As a result, an orally available, low molecular weight FimH antagonist was identified with the potential to reduce the colony forming units (CFU) in the urine by 2 orders of magnitude and in the bladder by 4 orders of magnitude. With FimH antagonist 16b, the great potential for the effective treatment of urinary tract infections with a new class of orally available antiinfectives could be demonstrated.