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  • Title: Design of a bivalent peptide with two independent elements of secondary structure able to fold autonomously.
    Author: Pantoja-Uceda D, Pastor MT, Salgado J, Pineda-Lucena A, Pérez-Payá E.
    Journal: J Pept Sci; 2008 Jul; 14(7):845-54. PubMed ID: 18247449.
    Abstract:
    This article describes a strategy to develop, starting from a de novo design, bivalent peptides containing two different (alpha-helix and beta-hairpin) and independent secondary-structure elements. The design was based on the use of conformationally restricted peptide libraries. Structural characterization by NMR revealed that the peptides were stable and did not show any long-range NOE interactions between the N-terminal beta-hairpin and the C-terminal alpha-helix. These results suggest that the two elements of secondary structure are stable and well folded.
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