David Aitken

David Aitken

Director of the ICMMO
Université Paris-Sud
Orsay Cedex
France
 david.aitken@u-psud.fr

Abstract

The Role of Heteroatoms in Dictating the Conformational Preferences of Peptide Foldamers

For 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.

Lecture Images

David Aitken presenting at APS2019 David Aitken presenting at APS2019 David Aitken presenting at APS2019