A Cyclic β-Strand Tripeptide with an α-Helix Like CD Spectrum
- 17 June 2009
- journal article
- letter
- Published by American Chemical Society (ACS) in Organic Letters
- Vol. 11 (14) , 3092-3095
Abstract
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.Keywords
This publication has 25 references indexed in Scilit:
- α-Turn Mimetics: Short Peptide α-Helices Composed of Cyclic Metallopentapeptide ModulesJournal of the American Chemical Society, 2004
- Synthesis and Conformational Studies of Dipeptides Constrained by Disubstituted 3-(Aminoethoxy)propionic Acid LinkersThe Journal of Organic Chemistry, 2004
- Vibrational Spectroscopic Detection of Beta- and Gamma-Turns in Synthetic and Natural Peptides and ProteinsChemical Reviews, 2003
- The synthesis and study of side‐chain lactam‐bridged peptidesPeptide Science, 2002
- Non-proline Cis peptide bonds in proteinsJournal of Molecular Biology, 1999
- Design and Enantioselective Synthesis of a Peptidomimetic of the Turn in the Helix−Turn−Helix DNA-Binding Protein MotifThe Journal of Organic Chemistry, 1997
- Phi/Psi-chology: Ramachandran revisitedStructure, 1996
- Small Peptides as Potent Mimetics of the Protein Hormone ErythropoietinScience, 1996
- Calibration of the angular dependence of the amide proton-Cα proton coupling constants, 3JHNα, in a globular proteinJournal of Molecular Biology, 1984
- CHARMM: A program for macromolecular energy, minimization, and dynamics calculationsJournal of Computational Chemistry, 1983