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A predominantly hydrophobic recognition of H‐antigenic sugars by winged bean acidic lectin: a thermodynamic study
Author(s) -
Srinivas V.R,
Bhanuprakash Reddy G,
Surolia Avadhesa
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00502-5
Subject(s) - isothermal titration calorimetry , chemistry , lectin , agglutinin , trisaccharide , oligosaccharide , titration , biochemistry , moiety , enthalpy , stereochemistry , organic chemistry , thermodynamics , physics
The thermodynamics of binding of winged bean ( Psophocarpus tetragonolobus ) acidic agglutinin to the H‐antigenic oligosaccharide (Fucα1‐2Galβ1‐4GlcNAc‐oMe) and its deoxy and methoxy congeners were determined by isothermal titration calorimetry. We report a relatively hydrophobically driven binding of winged bean acidic agglutinin to the congeners of the above sugar. This conclusion is arrived, from the binding parameters of the fucosyl congeners, the nature of the enthalpy‐entropy compensation plots and the temperature 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 fucosyl moiety of the H‐antigenic determinant.