Design of a bivalent peptide with two independent elements of secondary structure able to fold autonomously. |
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Authors: | David Pantoja-Uceda M Teresa Pastor Jesús Salgado Antonio Pineda-Lucena Enrique Pérez-Payá |
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Institution: | Department of Medicinal Chemistry, Centro de Investigación Príncipe Felipe, Avda Autopista del Saler, 16. Valencia, Spain. |
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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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Keywords: | bivalent peptides conformationally defined peptide design peptide libraries NMR spectroscopy |
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