COMPLEXATION OF BASIC-AMINO-ACIDS BY WATER-SOLUBLE CALIXARENE SULFONATES AS A STUDY OF THE POSSIBLE MECHANISMS OF RECOGNITION OF CALIXARENESULFONATES BY PROTEINS

The interactions of calixarene sulphonates with the basic amino acids arginine and lysine were studied by H-1 NMR spectroscopy. Strong elect rostatic binding occurs for calix[4]arene sulphonate with both lysine and arginine at pH 1 and 5. For the higher calixarenes, only weak inte ractions at the faces of the flattened macrocycles occur. This binding is in contrast to the inhibition of protein-protein interactions by t he calixarenes where the calix[6]arene and calix[8]arene sulphonates s how much stronger effects. (C) 1998 John Wiley & Sons, Ltd.