PMID: 3755041Mar 15, 1986Paper

Thermodynamic and kinetic studies on saccharide binding to soya-bean agglutinin

The Biochemical Journal
Musti J SwamyA Surolia

Abstract

The fluorescence of N-dansylgalactosamine [N-(5-dimethylaminonaphthalene-1-sulphonyl)galactosamine] was enhanced 11-fold with a 25 nm blue-shift in the emission maximum upon binding to soya-bean agglutinin (SBA). This change was used to determine the association constants and thermodynamic parameters for this interaction. The association constant of 1.51 X 10(6) M-1 at 20 degrees C indicated a very strong binding, which is mainly due to a relatively small entropy value, as revealed by the thermodynamic parameters: delta G = -34.7 kJ X mol-1, delta H = -37.9 kJ X mol-1 and delta S = -10.9 J X mol-1 X K-1. The specific binding of this sugar to SBA shows that the lectin can accommodate a large hydrophobic substituent on the C-2 of galactose. Binding of non-fluorescent ligands, studied by monitoring the fluorescence changes when they are added to a mixture of SBA and N-dansylgalactosamine, indicates that a hydrophobic substituent at the anomeric position increases the affinity of the interaction. The C-6 hydroxy group also stabilizes the binding considerably. Kinetics of binding of N-dansylgalactosamine to SBA studied by stopped-flow spectrofluorimetry are consistent with a single-step mechanism and yielded k+1 = 2.4 X 10(5) M-1 X ...Continue Reading

Citations

Jul 30, 2010·Protein Science : a Publication of the Protein Society·Eda CelikMatthew P DeLisa
Oct 31, 2001·European Journal of Biochemistry·R KenothM J Swamy
Mar 10, 2006·Organic & Biomolecular Chemistry·Sneha Sudha KomathMusti J Swamy
Jan 18, 2007·Bioconjugate Chemistry·Ponnusamy BabuAvadhesha Surolia
Mar 15, 2014·Bioconjugate Chemistry·Juan ZhouOlof Ramström

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