Intramolecular Crosslinking of an Optically Inactive 310-Helical Peptide: Stabilization of Structure and Helix Sense
datasetposted on 2008-01-16, 00:00 authored by Naoki Ousaka, Tomohiro Sato, Reiko Kuroda
Cooperative structural stabilization and the deceleration of chirality interconversion of an octapeptide helix are achieved by a single intramolecular side-chain crosslinking, as revealed by X-ray crystallography, 1H NMR spectroscopy, and computational analyses. The helical inversion is slow on the NMR time scale even at 80 °C. This is the first case of decelerated chirality inversion for helices based on the biological backbone, and the sequence -Api-Aib2-Api- bridged with p-phenylenediacetic acid may serve as a key structural unit for the design of optically active peptides composed of only achiral building blocks and/or a variety of peptides with enhanced structural rigidity.
1 H NMR spectroscopyIntramolecular Crosslinkingachiral building blocksstabilizationsequencecrosslinkingchirality inversionhelical inversionvarietyintramolecularNMR time scalehelicePeptidecrystallographybridgedphenylenediacetic acidrigiditydecelerationApiHelix Sense CooperativeanalysesStabilizationHelicaloctapeptide helixchirality interconversionOptically Inactive 3 10