Complexation of basic amino acids by water-soluble calixarene sulphonates as a study of the possiblemechanisms of recognition of calixarene sulphonates by proteins

The interactions of calixarene sulphonates with the basic amino acids arginine and lysine were studied by 1H NMR spectroscopy. Strong electrostatic binding occurs for calix[4]arene sulphonate with both lysine and arginine at pH 1 and 5. For the higher calixarenes, only weak interactions at the faces of the flattened macrocycles occur. This binding is in contrast to the inhibition of protein–protein interactions by the calixarenes where the calix[6]arene and calix[8]arene sulphonates show much stronger effects.