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Glycobiology Advance Access originally published online on June 16, 2006
Glycobiology 2006 16(9):822-832; doi:10.1093/glycob/cwl014
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© The Author 2006. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Evaluation of {alpha}-D-mannopyranoside glycolipid micelles–lectin interactions by surface plasmon resonance method

Bandaru Narasimha Murthy3, Nicolas Hans Voelcker2,4 and Narayanaswamy Jayaraman1,3

3 Department of Organic Chemistry, Indian Institute of Science, Bangalore 560 012, India; and 4 School of Chemistry, Physics, and Earth Sciences, Flinders University, Adelaide 5001, Australia


1 To whom correspondence should be addressed; e-mail: jayaraman{at}orgchem.iisc.ernet.in

2 To whom correspondence should be addressed; e-mail: voel0002{at}flinders.edu.au

Received on January 27, 2006; revised on May 3, 2006; accepted on June 9, 2006

It is established that achieving higher binding affinities in carbohydrate–protein interactions requires multivalent presentations of the sugar ligands at the receptor binding site. Several 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 (DLS) studies afforded details of the aggregation numbers and the hydrodynamic diameters of various glycolipid (GL) micelles. The GL 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. Furthermore, micelles formed from two-sugar containing GLs are able to elicit favorable kinetic association rate constants in comparison to the micelles constituted with one-sugar containing GLs. The kinetic rate constants across the micelles and the effect of the sugar valencies in the GLs are discussed.

Key words: carbohydrates / glycolipidskinetics / lectins / micelles / surface plasmon resonance


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