72656-05-4

Usage

Uses

Used in Organic Synthesis:
Methyl4,6-O-benzylidene-3-O-(b-D-glucopyranoside)-a-D-glucopyranoside is used as a key intermediate in organic synthesis for the development of various complex molecules and pharmaceutical compounds. Its unique structure allows for further functionalization and modification, making it a valuable building block in the synthesis of novel molecules with potential applications in different industries.
Used in Pharmaceutical Industry:
In the pharmaceutical industry, Methyl4,6-O-benzylidene-3-O-(b-D-glucopyranoside)-a-D-glucopyranoside is used as a starting material for the synthesis of glycosidic compounds, which have potential therapeutic applications. These compounds can be used as drug candidates for the treatment of various diseases, including cancer, infectious diseases, and metabolic disorders, due to their ability to interact with specific biological targets.
Used in Material Science:
Methyl4,6-O-benzylidene-3-O-(b-D-glucopyranoside)-a-D-glucopyranoside can also be used in material science for the development of novel materials with specific properties. Its unique structure and functional groups can be exploited to create materials with tailored properties, such as improved mechanical strength, thermal stability, or biocompatibility, which can be applied in various fields, including electronics, packaging, and medical devices.

Upstream product

• 70144-58-0 methyl (2,3,4,6-tetra-O-acetyl-α-D-mannopyranosyl)-(1->3)-4,6-O-benzylidene-α-D-mannopyranoside 
• 617-04-9 (2R,3S,4S,5S,6S)-2-(hydroxymethyl)-6-methoxytetrahydro-2H-pyran-3,4,5-triol 
• 1769-06-8 methyl 2,3,4,6-tetrakis-O-trimethylsilyl-α-D-mannopyranoside 
• 3162-96-7 methyl-4,6-O-phenylmethylene-α-D-mannopyranoside 

Relevant academic research and scientific papers

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.