Journal
ACS CHEMICAL BIOLOGY
Volume 9, Issue 3, Pages 613-616Publisher
AMER CHEMICAL SOC
DOI: 10.1021/cb4007979
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- Freie Universitat Berlin
- Wallonie-Bruxelles International
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The substitution of alpha-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 alpha-helical peptide and an alpha beta gamma-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 alpha-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 beta/gamma-segment. Gained results can be directly applied in the design of biologically relevant peptides containing beta- and gamma-amino acids.
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