title: Bio-inspired Herringbone Foldamers: Strategy for Changing the Structure of Helices.
abstract: Cyclic oligomers of azole peptides were isolated from a multitude of marine organisms and were used for a large number of molecular machines. As shown previously, oligomers derived from achiral imidazole amino acids fold into canonical helices. Here we show that a minor change, the introduction of a methyl group in the δ position, results in a significant change in the secondary structure of the corresponding oligomers. Instead of a canonical helix, a noncanonical herringbone helix is formed. In the latter, the slope along the helix changes its sign at least twice per turn. This strategy allows a remarkable change of the secondary structure via a small modification. By means of enantiomerically pure amino acids, we were able to control, for the first time, both the helicity of the helix and the form of the herringbone. The investigation of the underlying herringbone basic element and its folding to a noncanonical helix were conducted by NMR and CD spectroscopy, as well as by X-ray crystallography and quantum chemical calculations.
authors.affiliation: Institut für Organische Chemie, Universität Duisburg-Essen , Universitätsstr. 7, D-45117 Essen, Germany.
authors.forename: Abdulselam
authors.identifier: 0000-0003-3588-5737
authors.initials: A
authors.lastname: Adam
authors.affiliation: Institut für Organische Chemie, Universität Duisburg-Essen , Universitätsstr. 7, D-45117 Essen, Germany.
authors.forename: Gebhard
authors.identifier: 0000-0002-5427-7510
authors.initials: G
authors.lastname: Haberhauer
authors.affiliation: Institut für Organische Chemie, Universität Duisburg-Essen , Universitätsstr. 7, D-45117 Essen, Germany.
authors.forename: Christoph
authors.initials: C
authors.lastname: Wölper