Syntheses and Peptide-binding Properties of C₂-symmetric Metallomacrocycles

Receptor-like molecules with the well-defined binding cavity were successfully prepared by exploiting coordinate bond between transition metal and ligands. Furthermore, combinatorial binding studies revealed that these metal-templated self-assembling receptors have the highly selective peptide-binding properties. Further studies on the structures of complexes between receptors and peptide substrates, and the peptide-binding properties of the other related synthetic receptors are in progress in this laboratory. Over the last decade, much effort in supramolecular chemistry has been devoted to developing efficient synthetic receptors for peptides. Peptides as a substrate are interesting for their biological significance. There are many biochemical or medicinal processes, for examples enzymatic activity, antibody action and bacterial infections, in which a selective molecular interaction of peptide plays a decisive role. Thus study of synthetic receptors capable of selective binding to a specific peptide are not only useful for better understanding of biological processes, but also facilitate the design of sensors, catalysts and new medicinal therapeutics. Recently, metallomacrocycles which are self-assembled from a flexible ligand by exploiting metal-ligand coordinate bond are recognized as the emerging class of new synthetic receptors for peptide substrates. In metallo-macrocylic receptors, metal acts to maintain macrocyclic structure and thus makes the receptor preorganized for the effective complexation with the corresponding substrates