Studies on constructing metal-peptide networks using α/β-peptide containing metal-coordinating α-amino acid

Abstract

Metal peptide networks have received a lot of attention as one of the metal-organic coordinated architectures due to their distinctive and complicated structure as well as their applicability in various fields. In this thesis, we studied the foldamers with β, ββ, and βαβ modules (β = ACPC, α =Aib) containing methionine residues to create new MPNs. Met-foldamers adopted different secondary structures like sheet or helix depending on sequence. These series of foldamers revealed various MPNs. In addition, we confirmed that channel morphology can be regulated by replacing channel-oriented residues with α amino acids in the peptides of the channel-forming MPNs. Also, the α amino acid site, which acts as a metal binding site, was changed to glutamic acid, and studied whether the glutamic acid could expand to other analogs. We successfully transformed glutamic acid into a hydroxamic acid moiety and acridine ester moiety, and some of them revealed the possibility of metal coordinating ability in Ca (II) and Pd (II), respectively. This study will be a good example of how we can design and synthesize new MPNs and further, will expand the MPNs library.