Design of a bivalent peptide with two independent elements of secondary structure able to fold autonomously

This article describes a strategy to develop, starting from a de novo design, bivalent peptides containing two different (α‐helix and β‐hairpin) and independent secondary‐structure elements. The design was based on the use of conformationally restricted peptide libraries. Structural characterization...

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Bibliographic Details
Published in:Journal of peptide science 2008-07, Vol.14 (7), p.845-854
Main Authors: Pantoja‐Uceda, David, Pastor, M. Teresa, Salgado, Jesús, Pineda‐Lucena, Antonio, Pérez‐Payá, Enrique
Format: Article
Language:English
Subjects:
Amino Acid Sequence
bivalent peptides
conformationally defined
Models, Molecular
Molecular Sequence Data
NMR spectroscopy
Nuclear Magnetic Resonance, Biomolecular
peptide design
peptide libraries
Peptides - chemistry
Peptides - metabolism
Protein Folding
Protein Structure, Secondary
Protein Structure, Tertiary
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Summary:This article describes a strategy to develop, starting from a de novo design, bivalent peptides containing two different (α‐helix and β‐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 β‐hairpin and the C‐terminal α‐helix. These results suggest that the two elements of secondary structure are stable and well folded. Copyright © 2008 European Peptide Society and John Wiley & Sons, Ltd.
ISSN:1075-2617
1099-1387
DOI:10.1002/psc.1015