AI Article Synopsis
- The use of homologated amino acids in peptides generally reduces their thermal stability, but a study identified a specific interaction between an α-helical peptide and an αβγ-chimera that maintains stability.
- Selected peptides exhibited thermal stabilities similar to those made from only α-amino acids, thanks to specific bonding interactions explained through molecular dynamics simulations and mutational analysis.
- These findings offer valuable insights for designing biologically relevant peptides that incorporate β- and γ-amino acids.
Article 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.
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| http://dx.doi.org/10.1021/cb4007979 | DOI Listing |
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