This communication describes how the "quantized" size effect of dendrimers can be exploited towards a size selective binding mechanism for the inhibition of protein-protein binding.

Building on our previous results that revealed a sized based mechanism for dendrimer/protein binding, the mechanism of complexation is further probed using CD spectroscopy; the results demonstrate that dendrimer/protein binding is not accompanied by changes in the protein's structure and that binding takes place on the interfacial area/active site entrance.

It is known that dendrimers can bind proteins with good selectively. This selectivity comes about from an optimization based on matching the size of the dendrimer with the size of the protein's interfacial binding area. In this paper, we report how this selectivity can be moderated by the functionality on the surface of the dendrimer. Specifically, we describe the synthesis of amino acid functionalized dendrimers and the effect of functionality on the dendrimer's ability to bind and inhibit the enzymatic protein, chymotrypsin. The results show how dendrimer binding can be increased or decreased depending on the terminal functionality. These results will allow new ligands to be designed and synthesized, possessing increased and selective protein-binding abilities.

Summary: Our initial studies into protein binding using a series of dendrimers as size selective inhibitors have been described. Two different proteins, cytochromo‐c and chymotrypsin have been selected for these binding experiments.