Abstract
Conformations of three pairs of dehydropeptides with the opposite configuration of the ΔPhe residue, Boc-Gly-ΔZ/EPhe-Phe-p-NA (Z- p -NA and E- p -NA), Boc-Gly-ΔZ/EPhe-Phe-OMe (Z-OMe and E-OMe), and Boc-Gly-ΔZ/EPhe-Phe-OH (Z-OH and E-OH) were compared on the basis of CD and NMR studies in MeOH, TFE, and DMSO. The CD results were used as the additional input data for the NMR-based calculations of the detailed solution conformations of the peptides. It was found that Z- p -NA, E- p -NA, Z-OMe, and Z-OH adopt the β-turn conformations and E-OMe and E-OH are unordered. There are two overlapping type III β-turns in Z- p -NA, type II’ β-turn in E- p -NA, and type II β-turn in Z-OMe and Z-OH. The results obtained indicate that in the case of methyl esters and peptides with a free carboxyl group, ΔZPhe is a much stronger inducer of ordered conformations than ΔEPhe. It was also found that temperature coefficients of the amide protons are not reliable indicators of intramolecular hydrogen bonds donors in small peptides.
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Acknowledgments
We would like to thank prof. Andrzej Ejchart (Institute of Biochemistry and Biophysics, Polish Academy of Sciences) for making the 500 MHz Varian spectrometer available to us. The syntheses of peptides, performed by M. Makowski, were supported by the Wrocław Research Center EIT + under the project “Biotechnologies and advanced medical technologies––BioMed” (POIG 01.01.02-02-003/08-00 financed from the European Regional Development Fund (Operational Programme Innovative Economy, 1.1.2).
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The authors declare that they have no conflict of interest.
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Jaremko, M., Jaremko, Ł., Mazur, A. et al. Enhanced β-turn conformational stability of tripeptides containing ΔPhe in cis over trans configuration. Amino Acids 45, 865–875 (2013). https://doi.org/10.1007/s00726-013-1534-9
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DOI: https://doi.org/10.1007/s00726-013-1534-9