Characteristic Structural Parameters for the γ-Peptide 14-Helix: Importance of Subunit Preorganization

All wound up: Crystallographic data for a set of homologous peptides constructed from gabapentin and two to six preorganized γ‐amino acid residues (see crystal structure of the longest peptide) allow derivation of characteristic parameters for the γ‐peptide 14‐helix and establish guidelines for char...

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Veröffentlicht in:Angewandte Chemie International Edition 2011-06, Vol.50 (26), p.5843-5846
Hauptverfasser: Guo, Li, Zhang, Weicheng, Reidenbach, Andrew G., Giuliano, Michael W., Guzei, Ilia A., Spencer, Lara C., Gellman, Samuel H.
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Sprache:eng
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Zusammenfassung:All wound up: Crystallographic data for a set of homologous peptides constructed from gabapentin and two to six preorganized γ‐amino acid residues (see crystal structure of the longest peptide) allow derivation of characteristic parameters for the γ‐peptide 14‐helix and establish guidelines for characterizing 14‐helical folding. The results suggest that the substitution pattern of a γ‐residue has a profound effect on the propensity for 14‐helical folding.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201101301