Themed collection Foldamers


Display selection of peptide ligands for helical aromatic foldamers
Display selection allowed for the identification of peptides with a lariat structure that bind to aromatic foldamer helices both sequence-selectively and diastereoselectively.
Org. Biomol. Chem., 2025,23, 4641-4647
https://doi.org/10.1039/D5OB00228A

Synthesis and stability of collagen mimetic peptides featuring δ-heteroatom-substituted prolines
Substituting the central proline residue in a collagen mimetic peptide with δ-oxaproline affords a faster-folding analogue with equivalent triple helix stability.
Org. Biomol. Chem., 2025,23, 3097-3101
https://doi.org/10.1039/D5OB00176E

Interrogating the potential of helical aromatic foldamers for protein recognition
Exposing a helical foldamer bearing multiple side chains to all the proteins contained in a yeast cell lysate allowed for the identification of protein binders in the nanomolar range.
Org. Biomol. Chem., 2024,22, 9342-9347
https://doi.org/10.1039/D4OB01436G
Plasmid DNA delivery using arginine-rich cell-penetrating L/D-peptides containing α-aminoisobutyric acids
We investigate the effects of structural and conformational differences in cell-penetrating peptides on the formation of complexes with pDNA and their transfection efficiency, utilizing arginine-rich peptides that incorporate α-aminoisobutyric acid.
Org. Biomol. Chem., 2025,23, 5191-5196
https://doi.org/10.1039/D5OB00627A
An aromatic layered foldamer based on a (cis, cis)-squaramide: chiral induction and absolute structure
The meta-linked bissquaramides 8 and 9 were synthesized and spectroscopically characterized.
Org. Biomol. Chem., 2025,23, 4927-4933
https://doi.org/10.1039/D5OB00324E
Modulation of insulin receptor activation through controlled folding of peptide ligands
In this study, we synthesized and evaluated analogs of S597 and the IR antagonist Ins-AC-S2, replacing their native disulfide bridges with alternative linkages, which significantly reduced the agonistic potency of S597.
Org. Biomol. Chem., 2025,23, 4776-4781
https://doi.org/10.1039/D5OB00363F
Palindromic peptide foldamers: a strategy for structural stability and cellular uptake
A palindromic L-leucine/L-arginine peptide foldamer shows stable α-helicity and efficient cellular uptake, offering a promising strategy to enhance the stability and permeability of mid-sized peptide therapeutics.
Org. Biomol. Chem., 2025, Advance Article
https://doi.org/10.1039/D5OB00430F

cis-Amide promotion in α-ABpeptoid foldamers via triazolium side chains
Triazolium-type N-substituents in α-ABpeptoids stronlgy induce cis amide geometry, enhancing their conformational homogeneity.
Org. Biomol. Chem., 2025, Advance Article
https://doi.org/10.1039/D5OB00355E
A β-hairpin peptide derived from Aβ forms different oligomers in the crystal state and in aqueous solution
The supramolecular assembly of amyloidβ into soluble oligomers is critical Alzheimer's disease (AD) progression.
Org. Biomol. Chem., 2025,23, 3881-3893
https://doi.org/10.1039/D5OB00296F

Stabilization of optically inactive α-helices of peptidic foldamers through sequence control and i, i + 4 stapling
An optically-inactive α-helical peptide with a minimal hydrocarbon-based staple exhibits a P/M interconversion of 0.41 s−1 at 298 K.
Org. Biomol. Chem., 2025,23, 3366-3371
https://doi.org/10.1039/D5OB00244C

Solvatomorphism of a 2,6-pyridyldicarboxamide-based foldamer
A study into the influence of solvent on the conformational preferences and crystal packing behaviour of a foldamer is reported. The marked effect of solvent the dimensions of the cavity spaces adopted by these supramolecular scaffolds is identified.
Org. Biomol. Chem., 2025, Advance Article
https://doi.org/10.1039/D5OB00342C

Foldameric receptors with domain-swapping cavities capable of selectively binding and transporting monosaccharides
Foldameric receptors selectively bind and transport monosaccharide guests by forming dimeric complexes.
Org. Biomol. Chem., 2025,23, 2845-2853
https://doi.org/10.1039/D4OB02061H
Enhancing molecular diversity of peptoid oligomers using amino acid synthons
Unprotected amino acids can be used as reagents in the solid-phase synthesis of N-substituted glycine peptoid oligomers.
Org. Biomol. Chem., 2025,23, 1175-1183
https://doi.org/10.1039/D4OB01564A