concanavalin-a and betadex

concanavalin-a has been researched along with betadex* in 8 studies

Other Studies

8 other study(ies) available for concanavalin-a and betadex

ArticleYear
The Impact of Heteromultivalency in Lectin Recognition and Glycosidase Inhibition: An Integrated Mechanistic Study.
    Chemistry (Weinheim an der Bergstrasse, Germany), 2017, May-05, Volume: 23, Issue:26

    The vision of multivalency as a strategy limited to achieve affinity enhancements between a protein receptor and its putative sugar ligand (glycotope) has proven too simplistic. On the one hand, binding of a glycotope in a dense glycocalix-like construct to a lectin partner has been shown to be sensitive to the presence of a third sugar entity (heterocluster effect). On the other hand, several carbohydrate processing enzymes (glycosidases and glycosyltransferases) have been found to be also responsive to multivalent presentations of binding partners (multivalent enzyme inhibition), a phenomenon first discovered for iminosugar-type inhibitory species (inhitopes) and recently demonstrated for multivalent carbohydrate constructs. By assessing a series of homo- and heteroclusters combining α-d-glucopyranosyl-related glycotopes and inhitopes, it was shown that multivalency and heteromultivalency govern both kinds of events, allowing for activation, deactivation or enhancement of specific recognition phenomena towards a spectrum of lectin and glycosidase partners in a multimodal manner. This unified scenario originates from the ability of (hetero)multivalent architectures to trigger glycosidase binding modes that are reminiscent of those harnessed by lectins, which should be considered when profiling the biological activity of multivalent architectures.

    Topics: 1-Deoxynojirimycin; beta-Cyclodextrins; Binding, Competitive; Concanavalin A; Enzyme Inhibitors; Glycoside Hydrolases; Horseradish Peroxidase; Kinetics; Lectins; Peanut Agglutinin; Protein Binding

2017
Immobilization of multivalent glycoprobes on gold surfaces for sensing proteins and macrophages.
    The Analyst, 2016, Apr-07, Volume: 141, Issue:7

    The multivalent display of carbohydrates on the cell surface provides cooperative binding to improve the specific biological events. In addition to multivalency, the spatial arrangement and orientation of sugars with respect to external stimuli also trigger carbohydrate-protein interactions. Herein, we report a non-covalent host-guest strategy to immobilize heptavalent glyco-β-cyclodextrin on gold-coated glass slides to study multivalent carbohydrate-protein interactions. We have found that the localization of sugar entities on surfaces using β-cyclodextrin (β-CD) chemistry increased the avidity of carbohydrate-protein and carbohydrate-macrophage interactions compared to monovalent-β-CD sugar coated surfaces. This platform is expected to be a promising tool to amplify the avidity of sugar-mediated interactions on surfaces and contribute to the development of next generation bio-medical products.

    Topics: beta-Cyclodextrins; Cell Adhesion; Cell Line; Concanavalin A; Gold; Humans; Macrophages; Surface Properties

2016
Layer-by-layer deposition of vesicles mediated by supramolecular interactions.
    Langmuir : the ACS journal of surfaces and colloids, 2013, Aug-13, Volume: 29, Issue:32

    Vesicles are dynamic supramolecular structures with a bilayer membrane consisting of lipids or synthetic amphiphiles enclosing an aqueous compartment. Lipid vesicles have often been considered as mimics for biological cells. In this paper, we present a novel strategy for the preparation of three-dimensional multilayered structures in which vesicles containing amphiphilic β-cyclodextrin are interconnected by proteins using cyclodextrin guests as bifunctional linker molecules. We compared two pairs of adhesion molecules for the immobilization of vesicles: mannose-concanavalin A and biotin-streptavidin. Microcontact printing and thiol-ene click chemistry were used to prepare suitable substrates for the vesicles. Successful immobilization of intact vesicles through the mannose-concanavalin A and biotin-streptavidin motifs was verified by fluorescence microscopy imaging and dynamic light scattering, while the vesicle adlayer was characterized by quartz crystal microbalance with dissipation monitoring. In the case of the biotin-streptavidin motif, up to six layers of intact vesicles could be immobilized in a layer-by-layer fashion using supramolecular interactions. The construction of vesicle multilayers guided by noncovalent vesicle-vesicle junctions can be taken as a minimal model for artificial biological tissue.

    Topics: beta-Cyclodextrins; Biotin; Click Chemistry; Concanavalin A; Macromolecular Substances; Mannose; Microscopy, Fluorescence; Models, Molecular; Molecular Structure; Particle Size; Proteins; Streptavidin; Surface Properties

2013
Supramolecular control of oligosaccharide-protein interactions: switchable and tunable ligands for concanavalin A based on beta-cyclodextrin.
    Angewandte Chemie (International ed. in English), 2006, Aug-18, Volume: 45, Issue:33

    Topics: beta-Cyclodextrins; Concanavalin A; Ligands; Molecular Structure; Protein Binding

2006
Probing secondary carbohydrate-protein interactions with highly dense cyclodextrin-centered heteroglycoclusters: the heterocluster effect.
    Journal of the American Chemical Society, 2005, Jun-08, Volume: 127, Issue:22

    Comparison of the lectin-binding properties for highly dense beta-cyclodextrin-centered homo- and heteroglycoclusters with defined architecture provides evidence for the existence of strong synergic effects (heterocluster effect) on carbohydrate-protein recognition events.

    Topics: beta-Cyclodextrins; Carbohydrate Conformation; Carbohydrate Metabolism; Carbohydrates; Concanavalin A; Glucose; Lactose; Mannose; Models, Molecular; Thermodynamics

2005
Optimizing saccharide-directed molecular delivery to biological receptors: design, synthesis, and biological evaluation of glycodendrimer-cyclodextrin conjugates.
    Journal of the American Chemical Society, 2004, Aug-25, Volume: 126, Issue:33

    Dendritic beta-cyclodextrin (betaCD) derivatives bearing multivalent mannosyl ligands have been prepared and assessed for their binding efficiency toward the tetrameric plant lectin concanavalin A (Con A) and a mammalian mannose/fucose specific cell surface receptor from macrophages. The synthetic strategy exploits the reactivity between isothiocyanate and amine functionalities for the high-yielding assembly via thioureido links of the various building blocks, including host, spacer, branching, and carbohydrate ligand elements. The methodology has been applied to the preparation of a series of betaCD-polymannoside scaffolds differing in the ligand valency and geometry. This series allowed us to explore: (i) The effects of the glycodendritic architecture on the binding efficiency; (ii) the mutual influence between the cyclodextrin core and the glycodendritic moieties on the molecular inclusion and lectin-binding properties; and (iii) the consequence of inclusion complex formation, using the anticancer drug docetaxel (Taxotère) as a target guest, on biological recognition. Our results confirm the high drug solubilization capability of this new type of betaCD-dendrimer construct and indicate that subtle changes in the architecture of the conjugate may have important consequences on receptor affinity. Interestingly, the host-guest interaction can be monitored to build up supramolecular dynamic glycoclusters with increased lectin affinity. Alternatively, the information obtained from the structure-lectin-binding avidity-inclusion capability studies has been put forward in the design of very efficient molecular transporters for docetaxel based on glycodendritic CD dimers.

    Topics: beta-Cyclodextrins; Concanavalin A; Cyclodextrins; Docetaxel; Drug Carriers; Humans; Lectins; Lectins, C-Type; Macrophages; Mannose Receptor; Mannose-Binding Lectins; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Oligosaccharides; Paclitaxel; Receptors, Cell Surface; Taxoids

2004
Binding affinity properties of dendritic glycosides based on a beta-cyclodextrin core toward guest molecules and concanavalin A.
    The Journal of organic chemistry, 2001, Nov-16, Volume: 66, Issue:23

    The inclusion behavior and concanavalin A binding properties of hepta-antennated and newly synthesized tetradeca-antennated C-6-branched mannopyranosyl and glucopyrannosyl cyclomaltoheptaose (beta-cyclodextrin) derivatives have been evaluated by isothermal titration microcalorimetry and enzyme-linked lectin assay (ELLA), respectively. The synthesis of three first-order dendrimers based on a beta-cyclodextrin core containing 14 1-thio-beta-D-glucose, 1-thio-beta-mannose, and 1-thio-beta-rhamnose residues was performed following a convergent approach and involving (1) preparation of a thiolated bis-branched glycoside building block and (2) attachment of the building block onto heptakis(6-deoxy-6-iodo)-beta-cyclodextrin. Calorimetric titrations performed at 25 degrees C in buffered aqueous solution (pH 7.4) gave the affinity constants and the thermodynamic parameters for the inclusion complex formation of these beta-cyclodextrin derivatives with guests sodium 8-anilino-1-naphthalensulfonate (ANS) and 2-naphthalenesulfonate. The host capability of the persubstituted beta-cyclodextrins decreased with respect to the native beta-CD when sodium 2-naphthalenesulfonate was used as a guest and improved when ANS was used as a guest molecule. Heptavalent mannoclusters based on beta-CD cores enhance the lectin binding affinity due to the cluster effect; however, the increase of the valency from 7 to 14 ligands did not contribute to the improvement of the concanavalin A binding affinity. In addition, the synthesized hyperbranched mannoCDs lost completely the capability as a host molecules.

    Topics: beta-Cyclodextrins; Calorimetry; Carbohydrate Sequence; Concanavalin A; Cyclodextrins; Enzyme-Linked Immunosorbent Assay; Glycosides; Lectins; Molecular Sequence Data; Protein Binding; Receptors, Concanavalin A

2001
Dependence of concanavalin A binding on anomeric configuration, linkage type, and ligand multiplicity for thiourea-bridged mannopyranosyl-beta-cyclodextrin conjugates.
    Chembiochem : a European journal of chemical biology, 2001, Oct-01, Volume: 2, Issue:10

    Topics: beta-Cyclodextrins; Concanavalin A; Cyclodextrins; Glycoconjugates; Inhibitory Concentration 50; Ligands; Mannose; Molecular Conformation; Thiourea

2001