An unusual interstrand h-bond stabilizes the heteroassembly of helical αβγ-chimeras with natural peptides

Elisabeth K. Nyakatura, Raheleh Rezaei Araghi, Jérémie Mortier, Sebastian Wieczorek, Carsten Baldauf, Gerhard Wolber, Beate Koksch

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

The substitution of α-amino acids by homologated amino acids has a strong impact on the overall structure and topology of peptides, usually leading to a loss in thermal stability. Here, we report on the identification of an ideal core packing between an α-helical peptide and an αβγ-chimera via phage display. Selected peptides assemble with the chimeric sequence with thermal stabilities that are comparable to that of the parent bundle consisting purely of α-amino acids. With the help of MD simulations and mutational analysis this stability could be explained by the formation of an interhelical H-bond between the selected cysteine and a backbone carbonyl of the β/γ-segment. Gained results can be directly applied in the design of biologically relevant peptides containing β- and γ-amino acids.

Original languageEnglish (US)
Pages (from-to)613-616
Number of pages4
JournalACS Chemical Biology
Volume9
Issue number3
DOIs
StatePublished - Mar 21 2014
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine

Fingerprint Dive into the research topics of 'An unusual interstrand h-bond stabilizes the heteroassembly of helical αβγ-chimeras with natural peptides'. Together they form a unique fingerprint.

  • Cite this

    Nyakatura, E. K., Rezaei Araghi, R., Mortier, J., Wieczorek, S., Baldauf, C., Wolber, G., & Koksch, B. (2014). An unusual interstrand h-bond stabilizes the heteroassembly of helical αβγ-chimeras with natural peptides. ACS Chemical Biology, 9(3), 613-616. https://doi.org/10.1021/cb4007979