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The interactions of calixarene sulphonates with the basic amino acids arginine and lysine were studied by 1 H 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.
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