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Solution and solid state conformational preferences of a family of cyclic disulphide bridged tetrapeptides
Authors:Nadja Berger  Fee Li  Bert Mallick  J. Thomas Brüggemann  Wolfram Sander  Christian Merten
Affiliation:1. Fakult?t für Chemie und Biochemie, Lehrstuhl für Organische Chemie II, Ruhr‐Universit?t Bochum, Bochum, Germany;2. Fakult?t für Chemie und Biochemie, Lehrstuhl für Anorganische Chemie, Ruhr‐Universit?t Bochum, Bochum, Germany
Abstract:A set of cyclic tetrapeptides of the general form cyclo (Boc‐Cys‐Pro‐ X ‐Cys‐OMe) with X being L‐ / D‐Ala , L‐ / D‐Val , and L‐ / D‐Trp was synthesized. These peptides serve as model systems for structure elucidation in solution and feature a variety of structural motifs — namely a β‐turn with intramolecular hydrogen bonding interactions, cis/trans isomerism, and a disulphide bond. In this work, we performed a comprehensive structural analysis focussing on their β‐turn conformational preferences using NMR, VCD, and Raman spectroscopy. Our results provide evidence for a strong influence of a single stereocenter on the structures of the peptides whereas solvent polarity does not significantly affect them. Additionally, the solid state conformational preferences were studied by crystal structure analysis. Overall, a general trend for the conformational preferences of this set of peptides can be concluded from the results of the complementary investigations.
Keywords:vibrational circular dichroism  cyclic peptides  secondary structure analysis  NOE analysis
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