Multivalent carbohydrate recognition on a glycodendrimer-functionalized flow-through chip

Chembiochem. 2008 Jul 21;9(11):1836-44. doi: 10.1002/cbic.200800195.

Abstract

Dendrimers were fitted out with up to eight mannose moieties by "click" chemistry. They were subsequently attached to aluminum oxide chips via a spacer that was linked to the dendrimer core; this resulted in a microarray of glycodendrimers. Binding of the glycodendrimers to the fluorescent lectins ConA and GNA was observable in real time. In a single experiment it was possible to observe the multivalency enhancement or cluster effect in the binding event. This effect was small for ConA, in agreement with its widely spaced binding sites, whereas it was large for GNA, with its twelve much more closely spaced binding sites. The dendrimer-fitted chip represents a valuable screening tool for multivalency effects. Furthermore kinetic and thermodynamic data on binding events can be deduced. Inhibition experiments are also possible with the system as was shown for ConA with alpha-methyl mannose as the inhibitor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Agglutinins / metabolism
  • Aluminum Oxide / chemistry*
  • Carbohydrate Metabolism*
  • Carbohydrates / chemistry*
  • Concanavalin A / antagonists & inhibitors
  • Concanavalin A / metabolism
  • Dendrimers / chemistry*
  • Dendrimers / metabolism
  • Fluorescein-5-isothiocyanate / chemistry
  • Galanthus / metabolism
  • Kinetics
  • Mannose / chemistry
  • Methylmannosides / pharmacology
  • Microarray Analysis / methods*
  • Porosity
  • Protein Binding
  • Surface Properties
  • Thermodynamics

Substances

  • Agglutinins
  • Carbohydrates
  • Dendrimers
  • Methylmannosides
  • Concanavalin A
  • methylmannoside
  • Fluorescein-5-isothiocyanate
  • Aluminum Oxide
  • Mannose