Enhanced β-turn conformational stability of tripeptides containing Δphe in cis over trans configuration

Mariusz Jaremko*, Lukasz Jaremko, Adam Mazur, Maciej Makowski, Marek Lisowski

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)865-875
Number of pages11
JournalAmino Acids
Volume45
Issue number4
DOIs
StatePublished - Jul 1 2013

Keywords

  • Circular dichroism
  • Dehydropeptide conformation
  • Dehydropeptides
  • Dehydrophenylalanine configuration
  • Nuclear magnetic resonance
  • Temperature coefficients of amide protons

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Organic Chemistry

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