Director of the ICMMO
The Role of Heteroatoms in Dictating the Conformational Preferences of Peptide FoldamersFor two decades, peptides and peptidomimetic architectures have been front-stage in the fast-developing area of foldamer science. Regular helical folding patterns have been discovered, allowing others to be designed, in which the conformational preferences are governed by N–H•••O=C hydrogen bonding networks akin to those found in native peptide secondary structure. We have been examining the effects of other types of hydrogen bonds as tools to assist and/or direct helical peptide folding, in order to generate new and more sophisticated foldamer axioms in a controlled and predictable manner. In this presentation we will assess the lessons learned from recent studies conducted on short oligomers of cyclic β-amino acids which bear a nitrogen or oxygen heteroatom which is strategically implicated in N–H•••N(sp3) •and N–H•••O(sp3) • hydrogen bonding networks, then present out most recent observations on the previously unknown role of sulfur in sustaining predictable and tunable folding patterns in novel short peptide sequences.