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 Citations (Scopus)

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

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Amino Acids
Peptides
Thermodynamic stability
Hot Temperature
Bacteriophages
Amino Acid Substitution
Cysteine
Substitution reactions
Display devices
Topology

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine

Cite this

An unusual interstrand h-bond stabilizes the heteroassembly of helical αβγ-chimeras with natural peptides. / Nyakatura, Elisabeth K.; Rezaei Araghi, Raheleh; Mortier, Jérémie; Wieczorek, Sebastian; Baldauf, Carsten; Wolber, Gerhard; Koksch, Beate.

In: ACS Chemical Biology, Vol. 9, No. 3, 21.03.2014, p. 613-616.

Research output: Contribution to journalArticle

Nyakatura, EK, 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, vol. 9, no. 3, pp. 613-616. https://doi.org/10.1021/cb4007979
Nyakatura, Elisabeth K. ; Rezaei Araghi, Raheleh ; Mortier, Jérémie ; Wieczorek, Sebastian ; Baldauf, Carsten ; Wolber, Gerhard ; Koksch, Beate. / An unusual interstrand h-bond stabilizes the heteroassembly of helical αβγ-chimeras with natural peptides. In: ACS Chemical Biology. 2014 ; Vol. 9, No. 3. pp. 613-616.
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