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Issue 7, 2011
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The binding of polyvalent galactosides to the lectin Ricinus communis agglutinin 120 (RCA120): an ITC and SPR study

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Abstract

Mono- and polyvalent galactosides have been investigated with respect to their binding to the plant lectin Ricinus communis agglutinin 120 (RCA120). Thermodynamic parameters (Ka, ΔG, ΔH, ΔS and n) have been determined by isothermal titration calorimetry (ITC) and kinetics of binding (ka and kd) measured by surface plasmon resonance (SPR). ITC analysis using a single set of sites model found a non-statistical increase in avidity with increasing valency with the largest ligand displaying a greater than 20-fold increase in Ka compared to its monomeric precursor after correction for valency; binding was found to be enthalpically driven. SPR analysis supports the avidity increase but values of Ka observed were up to 100-fold greater than those measured by ITC. The large discrepancy between the two measurements is rationalized by the polyvalent–polyvalent interaction that is measured by SPR.

Graphical abstract: The binding of polyvalent galactosides to the lectin Ricinus communis agglutinin 120 (RCA120): an ITC and SPR study

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Supplementary files

Article information


Submitted
19 Jan 2011
Accepted
10 Mar 2011
First published
04 Apr 2011

Polym. Chem., 2011,2, 1552-1560
Article type
Paper

The binding of polyvalent galactosides to the lectin Ricinus communis agglutinin 120 (RCA120): an ITC and SPR study

S. G. Spain and N. R. Cameron, Polym. Chem., 2011, 2, 1552
DOI: 10.1039/C1PY00030F

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