Themed collection Foldamer Chemistry

This themed issue of NJC features a collection of papers highlighting the latest developments in foldamer chemistry.

Published data on peptide isolated and repetitive γ-turns are reviewed. Advancements in our laboratories on these 3D-structures are also presented.

A survey of crystal- and solution-structure information for macrocyclic peptides, illustrating common folding patterns and target binding effects.

Cis conformational properties of N,N′-dimethylurea and guanidine can be applied to construct foldamers with aromatic multilayers and dynamic helical conformations.

The photo-crosslinking of a coumarin-functionalized dipeptide hydrogel enhances the stability of the self-assembled nanofibers that comprise the hydrogel.

cis-2-Aminocyclohex-4-enecarboxylic acid can promote the α/β-peptide 11/9-helix in solution and in the crystal state.

A 15-residue aromatic oligoamide with a backbone of increased flexibility exhibits solvent- and temperature-dependent folding and highly cooperative conformational transition.

Snapshots from molecular dynamics simulations showcase how substituent positions and linkage types affect the secondary structure properties of fluorobenzene based helical arylamides.

This paper deals with the role of N-terminal proline in stabilizing the Ant–Pro zipper structure by the co-operative contribution of competing forces viz. hydrogen bonding, aromatic stacking and backbone chirality.

γ_n amino acid residues can be incorporated into structures in γ_n and hybrid sequences containing folded and extended α and δ residues.

The methodology allows for the preparation of enantiopure δ-substituted L-proline analogues bearing the side chain of proteinogenic residues.

A new class of α/β^2,3-peptides were synthesized from C-linked carbo-β^2,3-amino acids (β^2,3-Caas) and investigated to understand the impact of the side chains (allyl/propargyl) at the Cα-position on their conformations.

3₁₀ helical conformations that extend over 21 Å result when selected non-Aib terminal and central residues are incorporated into Aib-rich foldamers.

Varying the solvent offers a simple way to control superstructure polymorphism of a tri-β³-peptide-based supramolecular system.

These oligomers adopt a regular zig-zag strand-like secondary structure which does not rely on intra-residue 6-ring hydrogen bonds for stability.

The sodium ion-triggered extension and contraction motions along with photo-induced cis–trans isomerisation of a photoresponsive spiroborate-based double-stranded helicate were investigated.

A new β-hairpin mimic foldamer based on the assembly of a reverse turn inducer, a peptidomimetic strand, and a tetrapeptide sequence was prepared, and its conformation in solution was assessed by NMR and computational investigations.

Oligo-γ-peptides based on 2-aminocyclopentylacetic acid (γAc₅a) with a cyclopentyl constraint on the C^β–C^γ bond and homochiral (1S,2S) configurations preferentially adopt the right-handed 14-helix foldamers in the gas phase and in solution.