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An Unusual Interstrand H-Bond Stabilizes the Heteroassembly of Helical αβγ-Chimeras with Natural Peptides

MPG-Autoren
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Baldauf,  Carsten
Theory, Fritz Haber Institute, Max Planck Society;

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Zitation

Nyakatura, E. K., Araghi, R. R., Mortier, J., Wieczorek, S., Baldauf, C., Wolber, G., et al. (2014). An Unusual Interstrand H-Bond Stabilizes the Heteroassembly of Helical αβγ-Chimeras with Natural Peptides. ACS Chemical Biology, 9(3), 613-616. doi:10.1021/cb4007979.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0018-F6E1-C
Zusammenfassung
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.