The binding of monosaccharides to wheat germ agglutinin: fluorescence and NMR investigations.
The synthesis of N-acetyl- and N-trifluoroacetyl-glucosaminides was reported. The interaction of these compounds with wheat germ agglutinin, a plant lectin specific for N-acetyl-glucosamine and sialic acid, was investigated by two complementary approaches: 1H and 19F NMR, and fluorescence spectroscopy. This last technique relies on the existence of a competitive equilibrium involving the protein, the ligand and O-(methylumbelliferyl)-N-acetyl-glucosaminide, a fluorescent saccharide. The binding constants and the chemical shifts in the complex were determined and were related to the protein structure.
D055598:Chemical Phenomena; D002621:Chemistry; D007700:Kinetics; D037102:Lectins; D009682:Magnetic Resonance Spectroscopy; D009005:Monosaccharides; D013050:Spectrometry, Fluorescence; D013329:Structure-Activity Relationship; D013816:Thermodynamics; D014909:Wheat Germ Agglutinins
D037102:Lectins; D009005:Monosaccharides; D014909:Wheat Germ Agglutinins