21893-05-0Relevant articles and documents
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Whistler,Anisuzzaman
, p. 3823 (1969)
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Synthesis and surface-active properties of amphiphilic 6-aminocarbonyl derivatives of D-glucose
Maunier, Valerie,Boullanger, Paul,Lafont, Dominique,Chevalier, Yves
, p. 49 - 57 (1997)
Several 6-amido-6-deoxy derivatives of methyl α-D-glucopyranoside and D-glucopyranose were prepared via peracetylated 6-azido-6-deoxy or 6-deoxy-6-isocyanato intermediates. These compounds displayed high Krafft temperatures which could result from hydrogen bonding between NH and O-5. Their tensio-active properties above the Krafft temperature were compared with Hecameg (methyl 6-O-(N-heptylcarbamoyl)-α-D-glucopyranoside).
AMYLOID TARGETING AGENTS AND METHODS OF USING THE SAME
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Paragraph 00834, (2015/11/10)
Provided herein is the design and synthesis of novel molecular rotor fluorophores useful for detection of amyloid or amyloid like proteins. The fluorophores are designed to exhibit enhanced fluorescence emission upon associating with amyloid or amyloid like proteins as compared to unbound compound. Also disclosed herein are the methods for treating of diseases associated with an amyloid or amyloid like proteins.
Design and synthesis of hydrolytically stable multivalent ligands bearing thiodigalactoside analogues for peanut lectin and human galectin-3 binding
Cagnoni, Alejandro J.,Kovensky, José,Uhrig, María Laura
, p. 6456 - 6467 (2014/08/05)
Herein, we describe the design and synthesis of a novel family of hydrolytically stable glycoclusters bearing thiodigalactoside (TDG) analogues as recognition elements of β-galactoside binding lectins. The TDG analogue was synthesized by thioglycosylation of a 6-S-acetyl-α-d-glucosyl bromide with the isothiouronium salt of 2,3,4,6-tetra-O-acetyl-β-d-galactose. Further propargylation of the TDG analogue allowed the coupling to azido-functionalized oligosaccharide scaffolds through copper(I)-catalyzed azide-alkyne cycloaddition (CuAAC) under microwave activation. The final mono-, di-, and tetravalent ligands were resistant to enzymatic hydrolisis by Escherichia coli β-galactosidase. Binding affinities to peanut agglutinin and human galectin-3 were measured by isothermal titration calorimetry which showed Ka constants in the micromolar range as well as a multivalent effect. Monovalent ligand exhibited a binding affinity higher than that of thiodigalactoside. Docking studies performed with a model ligand on both β-galactoside binding lectins showed additional interactions between the triazole ring and lectin amino acid residues, suggesting a positive effect of this aromatic residue on the biological activity.