2872-56-2

Basic information

• Product Name: methyl 3-O-acetyl-4,6-O-benzylidene-α-D-mannopyranoside
• Synonyms: methyl 3-O-acetyl-4,6-O-benzylidene-α-D-mannopyranoside
• CAS NO: 2872-56-2
• Molecular Weight: 324.331
• Mol File: 2872-56-2.mol
• Article Data: 25

Chemical Properties

• CAS DataBase Reference: methyl 3-O-acetyl-4,6-O-benzylidene-α-D-mannopyranoside(CAS DataBase Reference)
• NIST Chemistry Reference: methyl 3-O-acetyl-4,6-O-benzylidene-α-D-mannopyranoside(2872-56-2)
• EPA Substance Registry System: methyl 3-O-acetyl-4,6-O-benzylidene-α-D-mannopyranoside(2872-56-2)

Safety Data

• Hazardous Substances Data: 2872-56-2(Hazardous Substances Data)

Upstream product

• 4148-58-7 (4aR,6S,7S,8R,8aS)-6-Methoxy-2-phenyl-hexahydro-pyrano[3,2-d][1,3]dioxine-7,8-diol 
• 97-72-3 2-Methylpropionic anhydride 
• 108-24-7 acetic anhydride 
• 75-36-5 acetyl chloride 
• 3162-96-7 methyl-4,6-O-phenylmethylene-α-D-mannopyranoside 
• 1769-06-8 methyl 2,3,4,6-tetrakis-O-trimethylsilyl-α-D-mannopyranoside 
• 617-04-9 (2R,3S,4S,5S,6S)-2-(hydroxymethyl)-6-methoxytetrahydro-2H-pyran-3,4,5-triol 
• 64-19-7 acetic acid 
• 3162-96-7 4,6-O-benzylidene-1-O-methyl-α-D-glucopyranoside 
• 141-78-6 ethyl acetate 
• 1449790-66-2 methyl 3-O-acetyl-4,6-O-benzylidene-2-O-(N-phenylcarbamoyl)-α-D-mannopyranoside 
• 162226-16-6 Acetic acid (2R,4aR,6S,7R,8S,8aR)-7-allyloxycarbonyloxy-6-methoxy-2-phenyl-hexahydro-pyrano[3,2-d][1,3]dioxin-8-yl ester 
• 1202384-87-9 C₁₈H₂₂O₉ 
• 1202384-86-8 C₁₈H₂₂O₉ 

Downstream Products

• 1449790-66-2 methyl 3-O-acetyl-4,6-O-benzylidene-2-O-(N-phenylcarbamoyl)-α-D-mannopyranoside 
• 98392-36-0 Methyl 2-O-acetyl-4,6-O-(phenylmethylene)-α-D-mannopyranoside 
• 2774-23-4 methyl 2-O-acetyl-4,6-O-benzylidene-α-D-glucopyranoside 
• 1163704-46-8 methyl 3-O-acetyl-4,6-O-benzylidene-α-D-glucopyranoside 
• 1441884-65-6 C₃₆H₄₃BrO₁₄ 
• 1441884-73-6 C₃₆H₄₃BrO₁₄ 
• 1423010-15-4 (2R,4aR,5aS,8aS,9S,9aR)-5a-methoxy-7-oxo-2-phenyloctahydrofuro[2',3':5,6]pyrano[3,2-d][1,3]dioxin-9-yl acetate 
• 1353896-04-4 methyl 4,6-O-benzylidene-2-O-diazoacetyl-3-O-acetyl-α-D-mannopyranoside 
• 1344677-53-7 C₃₈H₄₃N₃O₁₂ 
• 110715-29-2 methyl 4,6-O-benzylidene-2-O-methyl-α-D-glucopyranoside 
• 3150-15-0 methyl 2,3-anhydro-4,6-O-benzilidene-α-D-mannopyranoside 
• 23346-01-2 4,6-O-Benzylidene-1,2-dideoxy-D-erythro-hex-1-enopyranos-3-ulose 
• 6752-49-4 (4aR,6S,8aR)-6-Methoxy-2-phenyl-tetrahydro-pyrano[3,2-d][1,3]dioxin-8-one 
• 748151-09-9 methyl 2,3,4-tri-O-benzoyl-β-D-xylopyranosyl-(1-> 2)-3-O-acetyl-4,6-di-O-benzoyl-α-D-mannopyranoside 

Relevant articles and documents

Site-Selective Acylation of Pyranosides with Oligopeptide Catalysts

Herein, we report the oligopeptide-catalyzed site-selective acylation of partially protected monosaccharides. We identified catalysts that invert site-selectivity compared to N-methylimidazole, which was used to determine the intrinsic reactivity, for 4,6

Regioselective Sulfonylation/Acylation of Carbohydrates Catalyzed by FeCl3 Combined with Benzoyltrifluoroacetone and Its Mechanism Study

A catalytic amount of FeCl3 combined with benzoyl trifluoroacetone (Hbtfa) (FeCl3/Hbtfa = 1/2) was used to catalyze sulfonylation/acylation of diols and polyols using diisopropylethylamine (DIPEA) or potassium carbonate (K2CO3) as a base. The catalytic system exhibited high catalytic activity, leading to excellent isolated yields of sulfonylation/acylation products with high regioselectivities. Mechanism studies indicated that FeCl3 initially formed [Fe(btfa)3] (btfa = benzoyl trifluoroacetonate) with twice the amount of Hbtfa under basic conditions in the solvent acetonitrile at room temperature. Then, Fe(btfa)3 and two hydroxyl groups of the substrates formed a five- or six-membered ring intermediate in the presence of the base. The subsequent reaction between the cyclic intermediate and a sulfonylation reagent led to the selective sulfonylation of the substrate. All key intermediates were captured in the high-resolution mass spectrometry assay, therefore demonstrating this mechanism for the first time.

Binding of the Bacterial Adhesin FimH to Its Natural, Multivalent High-Mannose Type Glycan Targets

Multivalent carbohydrate-lectin interactions at host-pathogen interfaces play a crucial role in the establishment of infections. Although competitive antagonists that prevent pathogen adhesion are promising antimicrobial drugs, the molecular mechanisms underlying these complex adhesion processes are still poorly understood. Here, we characterize the interactions between the fimbrial adhesin FimH from uropathogenic Escherichia coli strains and its natural high-mannose type N-glycan binding epitopes on uroepithelial glycoproteins. Crystal structures and a detailed kinetic characterization of ligand-binding and dissociation revealed that the binding pocket of FimH evolved such that it recognizes the terminal α(1-2)-, α(1-3)-, and α(1-6)-linked mannosides of natural high-mannose type N-glycans with similar affinity. We demonstrate that the 2000-fold higher affinity of the domain-separated state of FimH compared to its domain-associated state is ligand-independent and consistent with a thermodynamic cycle in which ligand-binding shifts the association equilibrium between the FimH lectin and the FimH pilin domain. Moreover, we show that a single N-glycan can bind up to three molecules of FimH, albeit with negative cooperativity, so that a molar excess of accessible N-glycans over FimH on the cell surface favors monovalent FimH binding. Our data provide pivotal insights into the adhesion properties of uropathogenic Escherichia coli strains to their target receptors and a solid basis for the development of effective FimH antagonists.