Microcalorimetric indications for ligand binding as a function of the protein for galactoside-specific plant and avian lectins

• Published in: Biochimica et biophysica acta Vol. 1472; no. 1; pp. 191 - 196
• Main Authors: Bharadwaj, Satish, Kaltner, Herbert, Korchagina, Elena Y, Bovin, Nicolai V, Gabius, Hans-Joachim, Surolia, Avadhesha
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 18.10.1999
• Subjects: Agglutinin; Animals; Birds; Calorimetry - methods; Drug design; Galactoside; Galactosides - metabolism; Galectin; Galectins; Hemagglutinins - metabolism; Lectin; Ligands; Microcalorimetry; Plants - metabolism; Protein Binding; Thermodynamics; Galectin; Lectin; Thermodynamics; Agglutinin; Galactoside; Drug design; Microcalorimetry
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/S0304-4165(99)00120-8

The process cascade leading to the final accommodation of the carbohydrate ligand in the lectin’s binding site comprises enthalpic and entropic contributions of the binding partners and solvent molecules. With emphasis on lactose, N-acetyllactosamine, and thiodigalactoside as potent inhibitors of binding of galactoside-specific lectins, the question was addressed to what extent these parameters are affected as a function of the protein. The microcalorimetric study of carbohydrate association to the galectin from chicken liver (CG-16) and the agglutinin from Viscum album (VAA) revealed enthalpy–entropy compensation with evident protein type-dependent changes for N-acetyllactosamine. Reduction of the entropic penalty by differential flexibility of loops or side chains and/or solvation properties of the protein will have to be reckoned with to assign a molecular cause to protein type-dependent changes in thermodynamic parameters for lectins sharing the same monosaccharide specificity.