Themed collection Foldamer Chemistry

Intramolecular chirality transfer, amplification and solvent-mediated switching was observed in a series of random-coil peptide–dendron hybrids.

Foldamer sequences constructed by using trans-ABHC and β³-hSer residues produce β-H18 helix in a solvent- and concentration-dependent way.

The formamidoxime Z isomer coupled with the pyridylbiscarboxamide conformational codon fold into planar, curved units prone to self-assembly into channel-like structures, as examplified with original macrocycles.

Substituent effects on conformational behavior and electronic spectra have been examined in the first series of push–pull o-phenylenes.

Fluorescent PyrAc-(Deg)_n-O-(pNO₂)Bzl peptides exist as mixtures of fully-extended (right) and 3₁₀-helical conformers, the latter typical of (Aib)_n oligomers.

The reaction of sulfonyl peptides containing L- or D-configured Ser or Thr with bis(succinimidyl) carbonate in the presence of a catalytic amount of a base affords, in solution or in the solid phase, the corresponding peptides with one or two, consecutive or alternate oxazolidin-2-ones (Oxd).

The ¹⁵N-chemical shift tensor of urea bonds is determined and the bilayer topology of an antimicrobial oligourea analysed.

Click chemistry was used to introduce moieties as sterically demanding as monosaccharides into the Yaa position of collagen model peptides. The effect of different triazolyl derivatives as well as the configuration of the functionalized proline residue on the thermal stability of the collagen triple helices was examined.

One or more Gly-to-Lys replacements on the hydrophilic face of the peptide-template trichogin GA IV modulate its biological properties and promote a pH-mediated, reversible, 3₁₀- to α-helix transition.

A series of water-binding aquafoldamers have been studied in detail, illustrating their potential use for recognizing larger water clusters of diverse topologies and as synthetic water channels.

An extensive library of new, 14-helical, hexa β³-peptides demonstrates that appropriately stapled hexa-β³-peptides can allow for a number of variations, including staple size, location and functionalization, without significant perturbation of the 14-helix.

Conformational bias can be tuned from ribbon-type structures to β-sheet-like and helical motifs by intercalating suitable linear segments between cis-cyclobutane residues

Different capping groups have significant effects on spectral features/conformation of α,β-peptoids by CD, IR and NMR. These are most pronounced for shorter oligomers and are solvent dependent. This underlines the importance of considering capping groups for conformational studies.

The β-phenyl group attached to proline does not disrupt the β-turn propensity of the natural amino acid.

Flexible oligocholate foldamers transport carboxyfluorescein and glucose across lipid membranes in distinctively different mechanisms.

The participation of pyran oxygen of trans-3-aminopyran-2-carboxylic acid (APyC) in α/β-peptides resulting in 9/11-helix is envisaged to provide scope for new designs.

Benzamide-derived oligomers fold into compact conformations to complex aromatic and aliphatic carboxylate anions though multiple intermolecular N–H⋯O and C–H⋯O hydrogen bonds, and display helical chirality upon binding chiral glutamic acid dianion.

The Kulinkovich–de Meijere reaction provides non-racemic trans cyclopropylamines, which are converted into enantiomerically pure N-Boc protected β,γ-methano-GABA derivatives.

A solvent-free aza–Michael addition leading to new substituted β-aminocyclobutanecarboxylic acid derivatives and the reactivity of these donor–acceptor substituted cyclobutanes is described.

The conformational preferences of two lipopeptides C_n²H_(2n+1)CO-L-Phe-D-Oxd-OBn or C_n²H_(2n+1)CO-D-Phe-L-Oxd-OBn with n = 5 or 11 have been analyzed with solid-state ²H and ¹³C NMR techniques.

Regio- and stereoselective approaches to fluorinated alicyclic β-amino esters has been developed.