Solution and solid state conformational preferences of a family of cyclic disulphide bridged tetrapeptides. Issue 1 (January 2017)

• Record Type: Journal Article
• Authors: Berger, Nadja; Li, Fee; Mallick, Bert; Brüggemann, J. Thomas; Sander, Wolfram; Merten, Christian
• Other Names: Wemmer David sponsoringEditor.
• Is Part Of: Biopolymers. Volume 107:Issue 1(2017)
• Page Start: 28
• Page End: 34
• Publication Date: 2017-01
• Subjects: vibrational circular dichroism -- cyclic peptides -- secondary structure analysis -- NOE analysis; Biopolymers -- Periodicals; Peptides -- Periodicals; Spectrum analysis -- Periodicals; 572.33
• DOI: 10.1002/bip.22986
• Languages: English
• ISSNs: 0006-3525

Abstract

Abstract: A set of cyclic tetrapeptides of the general form cyclo (Boc‐Cys‐Pro‐X ‐Cys‐OMe) withX beingL‐ /D‐Ala, L‐ /D‐Val, andL‐ /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.