Combining biological structures and molecular self-assembly lead to ordered nanostructures

The bio activities of peptides encrypted in major food proteins are latent until released and activated by enzymatic electrolysis or food processing. The study of conformational properties of synthetic homologues of these bioactive peptides allows us to identify the biological structure. Peptide assembly structures have been widely exploited in fabricating materials promising for bioapplication. Peptides can self-organize into various highly ordered supramolecular architectures. Detailed studies of the molecular mechanism by which these versatile building blocks assemble can guide the design of peptide architectures with desired structure and functionality. It has been revealed that peptide assembly structures are highly sequence-dependent and sensitive to amino acid composition, the chirality of peptide and amino acid residues, and external factors, such as solvent, pH, and temperature. Combining biological structures and self-assembling in synthetic heterochiral peptides provides a powerful means to direct biological supramolecular materials formation. The creation of synthetic molecules that enable precise control over spacing and functionalization provides opportunities across diverse disciplines. Key requirements of functionalizable oligomeric scaffolds include the specific control of their molecular properties where the correct balance of flexibility and rigidity must be maintained in addition to the prerequisite of defined length. In this report, we describe our use of peptide model systems that fold cooperatively yet are small enough to be chemically synthesized to measure such quantities.