Motivated by the important roles played by the specific secondary structural domains of proteins, enormous efforts have been devoted to the design of structurally well-defined synthetic peptides. These investigations are aimed at gaining a deeper understanding of the mechanism of protein folding and of biochemical processes, generating molecules with potential biological applications, and developing novel materials. Various strategies have been exploited to design the controlled structures of peptides such as cyclization, insertion of β-amino acids, disulfide bonds, D-amino acids, or molecular scaffold in the peptide backbone.
In our research, we are exploiting ferrocene (Fc) which has recently been recognized for its ability to induce secondary structures and supramolecular arrangements to its peptide conjugates. Along with its ability to function as a molecular scaffold, Fc has fully reversible electrochemical behavior. The combination of these two inherent properties can enable preparation and the investigation of various electrochemical properties and molecular recognition behavior of specific structural peptides. We have developed methodologies that allow the incorporation of Fc derivatives (and other probe molecules) into a peptidic environment under mild conditions and are exploiting our approach for the design of novel peptide foldamers, to probe electron transfer, and mimic biological functions. In particular, we are interested in the design of sheet-like foldamers, some of which assemble into larger supramolecular structures.
Ongoing research efforts include:
a) the design of peptides that can interact with beta-amyloid, a causative agent for Alzheimer’s disease
b) stimuli responsive conjugates
c) peptide gels