A Cyclic β-Strand Tripeptide with an α-Helix Like CD Spectrum

A protein α-helix is defined by 3.6 amino acids per turn. Cyclization of the tripeptide Alanine-Leucine-Glutamate through a side chain to the N-terminus lactam bond produces cyclo-(1,3)-[ALE]-NH2 which displays a circular dichroism spectrum typical of an α-helix backbone. However, proton NMR spectra show a novel cyclic peptide featuring two non-hydrogen-bonded antiparallel β-strands connected by an Ala-Leu cis-amide bond. This example highlights that the common practice of characterizing α-helices by CD spectra alone can be misleading.