Macromolecular recognition: Effect of multivalency in the inhibition of binding of yeast mannan to concanavalin A and pea lectins by mannosylated dendrimers

Pagé, Daniel; Zanini, Diana; Roy, René

doi:10.1016/s0968-0896(96)00177-0

Cited by 139 publications

(47 citation statements)

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“…The relative lack of synergism in this study and in the present work may relate to the geometry of the dendrimers. PAMAM dendrimers have a spherical shape, whereas Pagé et al (1996) found that an unsymmetrical 16-mer glycodendrimer was approx. 600-fold more potent than methyl α-D-mannopyranoside in an experiment similar to that of Ashton et al (1998).…”

Section: Discussionmentioning

confidence: 99%

“…Thus, a 16-mer glycodendrimer with terminal mannoside residues was approx. 600-and 2000-fold more potent than methyl α-D-mannopyranoside as an inhibitor of binding of yeast mannan to con A and pea lectin respectively (Pagé et al, 1996). The present study therefore evaluated carbohydrate-substituted dendrimers, as well as monovalent carbohydrates, as inhibitors of ricin B-chain activity.…”

Section: Introductionmentioning

confidence: 99%

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Monovalent and polyvalent carbohydrate inhibitors of ricin binding to a model of the cell-surface receptor

et al. 2006

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A selection of galactose and lactose analogues was evaluated for their potency in inhibiting the binding of ricin to immobilised asialofetuin, which is a model of the cell-surface receptor for ricin. The aim was to identify compounds that could be used as antagonists of ricin toxicity in vivo, and as more selective, and therefore safer, antitoxins. Although one of these analogues had been identified by molecular modelling in a previous study as a potentially potent inhibitor, it and the other carbohydrates studied were less effective than galactose and lactose themselves (I(50) = 1.39 and 0.74 mM, respectively). In an attempt to increase the potency of carbohydrate-based inhibitors, galactose was coupled to the surface of dendrimers. No synergistic interactions were observed from this multivalent approach. Encouraging results, however, were obtained with a self-assembled lyotropic mesophase gel containing novel synthetic galactose-based surfactants, which was able to sequester ricin from aqueous solution in a 2-phase system.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Monovalent and polyvalent carbohydrate inhibitors of ricin binding to a model of the cell-surface receptor

et al. 2006

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“…Mannose-containing dendrimers based on oligolysyl structures were prepared as described elsewhere. [8] Structures of these compounds are shown in Schemes 1 and 2.…”

Section: Methodsmentioning

confidence: 99%

“…All these compounds have also been used in many lectin studies. [6,7] L-Lysine-based mannose dendrimers have been used in the study of legume lectins, [8] and their structural designs are given in Scheme 2. DP-2, DP-4, DP-8, and DP-16 dendrimers contain backbones consisting of 1, 3, 7, and 15 interconnected lysyl residues as scaffolds that will provide 2, 4, 8, and 16 terminal amino groups, respectively, through which the mannosides are linked.…”

Section: Neoglycoproteins and Other Multivalent Mannosidesmentioning

confidence: 99%

Inhibition of Adhesion of Type 1 Fimbriated Escherichia coli to Highly Mannosylated Ligands

et al. 2002

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“…In contrast to glycopeptides, highly flexible neoglycoconjugates [114] do not show high affinity due to the large entropic penalty. [115,116] The principle of glycopeptides mimicking oligosaccharides was consolidated through binding studies with an array of phosphorylated glycopeptides and the divalent mannose 6-phosphate receptor. [26] The structural similarity between the oligosaccharide and the most active glycopeptide ligand was supported by molecular dynamics (Figure 8).…”

Section: Glycopeptides As Oligosaccharide Mimeticsmentioning

confidence: 99%

Glycopeptide and Oligosaccharide Libraries

Hilaire

Meldal

2000

Angew. Chem. Int. Ed.

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Despite the burgeoning interest in the various biological functions and consequent therapeutic potential of the vast number of oligosaccharides found in nature on glycoproteins and cell surfaces, the development of combinatorial carbohydrate chemistry has not progressed as rapidly as expected. The reason for this imbalance is rooted in the difficulty of oligosaccharide assembly and analysis that renders synthesis a rather cumbersome endeavor. Parallel approaches that generate series of analogous compounds rather than real libraries have therefore typically been used. Since generally low affinity is obtained for interactions between carbohydrate receptors and modified oligosaccharides designed as mimetics of natural carbohydrate ligands, glycopeptides have been explored as alternative mimics. Glycopeptides have been proven in many cases to be superior ligands with higher affinity for a receptor than the natural carbohydrate ligand. High-affinity glycopeptide ligands have been found for several types of receptors including the E-, P-, and L-selectins, toxins, glycohydrolases, bacterial adhesins, and the mannose-6-phosphate receptor. Furthermore, the assembly of glycopeptides is considerably more facile than that of oligosaccharides and the process can be adapted to combinatorial synthesis with either glycosylated amino acid building blocks or by direct glycosylation of peptide templates. The application of the split and combine approach using ladder synthesis has allowed the generation of very large numbers of compounds which could be analyzed and screened for binding of receptors on solid phase. This powerful technique can be used generally for the identification and analysis of the complex interaction between the carbohydrates and their receptors.

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Macromolecular recognition: Effect of multivalency in the inhibition of binding of yeast mannan to concanavalin A and pea lectins by mannosylated dendrimers

Cited by 139 publications

References 50 publications

Monovalent and polyvalent carbohydrate inhibitors of ricin binding to a model of the cell-surface receptor

Monovalent and polyvalent carbohydrate inhibitors of ricin binding to a model of the cell-surface receptor

Inhibition of Adhesion of Type 1 Fimbriated Escherichia coli to Highly Mannosylated Ligands

Glycopeptide and Oligosaccharide Libraries

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