Metal-coordination-directed macrocyclic complexes, in which macrocyclic architectures are
formed by metal-ligand coordination interactions, have emerged as attractive …

α/γ-Peptide foldamers containing either γ4-amino acid residues or ring-constrained γ-amino
acid residues have been reported to adopt 12-helical secondary structure in nonpolar …

Macrocyclic peptides are an important class of bioactive substances. When inserting an
aromatic foldamer segment in a macrocyclic peptide, the strong folding propensity of the …

We present the first examples of atomic-resolution crystal data for the β-peptide 12/10-helix
from oligomers of cis-2-aminocyclohexane carboxylic acid (cis-ACHC) with alternating …

We explored trans-and cis-2-aminocycloheptanecarboxylic acid (ACHpC) as potential
building blocks for helical foldamers. trans-ACHpC does not show sufficient folding …

We describe the synthesis of trihydroxylated cyclohexane β-amino acids from (−)-shikimic
acid, in their cis and trans configuration, and the incorporation of the trans isomer into a trans …

The 11/9-helix is among the most stable and non-traditional helical structures for α/β-
peptides with alternating residue types. The effect of side chain groups of α-residues and β3 …

The α/β-peptide 11/9-helix and the β-peptide 12/10-helix belong to “mixed” helices, in which
two types of hydrogen bonds with opposite directionality alternate along the helical axis. cis …

Abstract The 11/9‐helix is one of nontraditional helices available to α/β‐peptides with
alternating residue types. Several β‐amino acid residues are known to promote 11/9‐helical …

α/β‐Peptide 11/9‐helix is an unconventional helical structure in which 11‐and 9‐membered
ring hydrogen bonds alternate along the helical axis. We have examined the interplay and …