Abstract
Sequential peptides containing Z-dehydrophenylalanine (ΔZPhe) residues, Boc-(L-Leu-ΔZPhe)n-L-Leu-OMe (n=2–6), were synthesized, and their conformations in solution were investigated using 1H NMR and CD spectroscopy. Tridecapeptide (n=6) was shown to adopt a helical conformation in CDCl3 by observation of successive NiH↔Ni+1H nuclear Overhauser effects. Solvent accessibility of NH resonances for peptide n=6 in CDCl3 indicated that all the NH groups except those belonging to the N-terminal Leu-ΔZPhe moiety participate in intramolecular hydrogen bonding. Similar accessibility was observed for peptides n=2–5. Thus, peptides n=2–6 in CDCl3 show a (i+3)→i intramolecular hydrogen bonding pattern characteristic of a 310-helix. CD spectra of peptides n=3–6 in chloroform showed exciton couplets around 280 nm with a negative peak at longer wavelengths, corresponding to a right-handed helical sense. ΔZPhe residue was shown to be effective to design a 310-helical-type backbone using sequential peptidcs of (X-ΔZPhe) unit.
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Inai, Y., Hasegawa, K., Hirabayashi, T. et al. Design of a Helical Backbone. Conformation of Sequential Tridecapeptide Containing Z-Dehydrophenylalanine Residues. Polym J 28, 238–245 (1996). https://doi.org/10.1295/polymj.28.238
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DOI: https://doi.org/10.1295/polymj.28.238
