The past several decades have witnessed great progress in the understanding of the high-
order structure of biomacromolecules. Currently, it is well-recognized that folding of proteins …

We explore strategies to enhance conformational ordering of N-substituted glycine peptoid
oligomers. Peptoids bearing bulky N-alkyl side chains have previously been studied as …

Conformationally ordered synthetic oligomers, also called “foldamers”, have attracted
considerable attention in recent years owing to their ability to mimic the structural …

A new helical aromatic oligoamide foldamer, bearing triethyleneglycol side chains for
solubility in a broad range of media, was prepared. The stability of the helical conformation …

Here we report the synthesis and characterization of four quinoline-derived foldamers with
increasing oligomeric length; dimer O2P, tetramer O4P, pentamer O5P, and nonamer O9P …

Helicity is a widespread characteristic of the secondary structure of peptides: those built of L-
amino acids typically adopt right-handed helical structures, even when most of the chain is …

The synthesis of quinoline-derived helically folded aromatic oligoamides functionalized by
various chiral functions at their N-terminus is reported. When a (1 S)-(−)-camphanyl moiety …

Synthetic helical aromatic amide foldamers and in particular those based on quinolines
have recently attracted much interest due to their capacity to adopt bioinspired folded …

Much effort is being devoted to develop oligomers that adopt stable helical conformations
and mimic the structures of folded biopolymers.[1] For example, bio-inspired helical …

Foldamer sequences that adopt tertiary helix‐turn‐helix folds mediated by helix‐helix
hydrogen bonding in organic solvents have been previously reported. In an attempt to create …