Effect of the Δphe residue configuration on a didehydropeptides conformation: A combined CD and NMR study

Marek Lisowski*, Lukasz Jaremko, Mariusz Jaremko, Adam Mazur, Rafał Latajka, MacIej Makowski

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

Conformations of two pairs of dehydropeptides with the opposite configuration of the ΔPhe residue, Boc-Gly-ΔZPhe-Gly-Phe- OMe (Z-OMe), Boc-Gly-ΔEPhe-Gly-Phe-OMe (E-OMe), Boc-Gly-ΔZPhe-Gly-Phe-p-NA (Z-p-NA), and Boc-Gly- ΔEPhe-Gly-Phe-p-NA (E-p-NA) were compared on the basis of CD and NMR studies in MeOH, trifluoroethanol (TFE), MeCN, chloroform, and dimethylsulfoxide (DMSO). The CD results were used as the additional input data for the NMR-based determination of the detailed solution conformations of the peptides. It was found that E-OMe is unordered and Z-OMe, Z-p-NA, and E-p-NA adopt the β-turn conformation. There are two overlapping β-turns in each of those peptides: type II and type III′ in Z-OMe and Z-p-NA, and two type III in E-p-NA. The ordered structure-inducing properties of ΔZPhe and ΔEPhe in the peptides studied depend on the C-terminal blocking group. In methyl esters, the ΔZPhe residue is a strong inducer of ordered conformations whereas the ΔEPhe one has no such properties. In p-nitroanilides, both isomers of ΔPhe cause the peptides to adopt ordered structures to a similar extent.

Original languageEnglish (US)
Pages (from-to)1055-1064
Number of pages10
JournalBiopolymers
Volume93
Issue number12
DOIs
StatePublished - Dec 1 2010

Keywords

  • circular dichroism
  • dehydropeptide conformation
  • dehydropeptides
  • dehydrophenylalanine configuration
  • nuclear magnetic resonance

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Biomaterials
  • Organic Chemistry

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