Abstract
Mono- and polyvalent galactosides have been investigated with respect to their binding to the plant lectin Ricinus communis agglutinin 120 (RCA 120). 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.
| Original language | English |
|---|---|
| Pages (from-to) | 1552-1560 |
| Number of pages | 9 |
| Journal | Polymer Chemistry |
| Volume | 2 |
| Issue number | 7 |
| DOIs | |
| Publication status | Published - Jul 2011 |
| Externally published | Yes |
Cite this
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The binding of polyvalent galactosides to the lectin Ricinus communis agglutinin 120 (RCA120) : An ITC and SPR study. / Spain, Sebastian G.; Cameron, Neil R.
In: Polymer Chemistry, Vol. 2, No. 7, 07.2011, p. 1552-1560.Research output: Contribution to journal › Article › Research › peer-review
TY - JOUR
T1 - The binding of polyvalent galactosides to the lectin Ricinus communis agglutinin 120 (RCA120)
T2 - An ITC and SPR study
AU - Spain, Sebastian G.
AU - Cameron, Neil R.
PY - 2011/7
Y1 - 2011/7
N2 - Mono- and polyvalent galactosides have been investigated with respect to their binding to the plant lectin Ricinus communis agglutinin 120 (RCA 120). 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.
AB - Mono- and polyvalent galactosides have been investigated with respect to their binding to the plant lectin Ricinus communis agglutinin 120 (RCA 120). 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.
UR - http://www.scopus.com/inward/record.url?scp=80855127420&partnerID=8YFLogxK
U2 - 10.1039/c1py00030f
DO - 10.1039/c1py00030f
M3 - Article
VL - 2
SP - 1552
EP - 1560
JO - Polymer Chemistry
JF - Polymer Chemistry
SN - 1759-9954
IS - 7
ER -