Glycobiology Advance Access published online on June 16, 2006
Glycobiology, doi:10.1093/glycob/cwl014
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1 Department of Organic Chemistry, Indian Institute of Science, Bangalore 560 012, India
* To whom correspondence should be addressed. It is established that achieving higher binding affinities in carbohydrate-protein interactions requires multivalent presentations of the sugar ligands at the receptor binding site. Many inhibition, calorimetric, mass balance and other studies have reiterated the beneficial effects of molecular level clustering of the sugar ligands for tight binding to the receptors. We have undertaken an effort to study the multivalent effects involving larger assemblies, represented by micelles, and their lectin interactions. The micelles were constituted with monomer bearing one- or two-sugar moieties at the monomolecular level and with varying the distances between the sugar moieties. Micellar aggregation studies and dynamic light scattering studies afforded details of the aggregation numbers and the hydrodynamic diameters of various glycolipid micelles. The glycolipid micelles were used as analytes of surface plasmon resonance (SPR) experiments on a lectin concanavalin A (Con A) immobilized surface. SPR studies of the micelle-lectin interactions demonstrate that the ligand-receptor binding can be fit into the bivalent analyte model of interaction. Further, micelles formed from two-sugar containing glycolipids are able to elicit favorable kinetic association rate constants in comparison to the micelles constituted with one-sugar containing glycolipids. The kinetic rate constants across the micelles and the effect of the sugar valencies in the glycolipids are discussed.
Received January 27, 2006
Revised May 4, 2006
Accepted June 9, 2006
Article
Evaluation of
Bandaru Narasimha Murthy 1,
Nicolas Hans Voelcker 2,
and
Narayanaswamy Jayaraman 1 *
-D-Mannopyranoside Glycolipid Micelles-Lectin Interactions by Surface Plasmon Resonance Method
2 School of Chemistry, Physics and Earth Sciences, Flinders University, Adelaide 5001, Australia
Narayanaswamy Jayaraman, E-mail: jayaraman{at}orgchem.iisc.ernet.in
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