A predominantly hydrophobic recognition of H-antigenic sugars by winged bean acidic lectin: a thermodynamic study

The thermodynamics of binding of winged bean (Psophocarpus tetragonolobus) acidic agglutinin to the H-antigenic oligosaccharide (Fuc alpha 1-2Gal beta 1-4GlcNac-oMe) and its deoxy and methoxy congeners were determined by isot hermal titration calorimetry, We report a relatively hydrophobically driven binding of winged bean acidic agglutinin to the congeners of the above sug ar. This conclusion is arrived, from the binding parameters of the fucosyl congeners, the nature of the enthalpy-entropy compensation plots and the te mperature dependence of binding enthalpies of some of the congeners, Thus, the binding site of winged bean acidic agglutinin must be quite extended to accommodate the trisaccharide, with non-polar loci that recognize the fuco syl moiety of the H-antigenic determinant. (C) 1999 Federation of European Biochemical Societies.