Conformationally Programmable Chiral Foldamers with Compact and Extended Domains Controlled by Monomer Structure

Zachariah Lockhart, Peter Knipe

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Foldamers are an important class of abiotic macromolecules, with potential therapeutic applications in the disruption of protein–protein interactions. The majority adopt a single conformational motif such as a helix. A class of foldamer is now introduced where the choice of heterocycle within each monomer, coupled with a strong conformation‐determining dipole repulsion effect, allows both helical and extended conformations to be selected. Combining these monomers into hetero‐oligomers enables highly controlled exploration of conformational space and projection of side‐chains along multiple vectors. The foldamers were rapidly constructed via an iterative deprotection‐cross‐coupling sequence, and their solid‐ and solution‐phase conformations were analysed by X‐ray crystallography and NMR and CD spectroscopy. These molecules may find applications in protein surface recognition where the interface does not involve canonical peptide secondary structures.
Original languageEnglish
Pages (from-to)8478-8482
JournalAngewandte Chemie International Edition
Issue number28
Early online date12 Jun 2018
Publication statusPublished - 09 Jul 2018



  • conformational analysis
  • foldamers
  • oligomerization
  • protein-protein interactions

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