6533b830fe1ef96bd1297ba2
RESEARCH PRODUCT
Design of a bivalent peptide with two independent elements of secondary structure able to fold autonomously.
M. Teresa PastorJesus SalgadoDavid Pantoja-ucedaEnrique Pérez-payáAntonio Pineda-lucenasubject
Models MolecularProtein FoldingStereochemistryMolecular Sequence DataPeptideBiochemistryBivalent (genetics)Protein Structure Secondarybivalent peptidesNMR spectroscopyStructural BiologyDrug DiscoveryAmino Acid SequenceMolecular BiologyProtein secondary structureNuclear Magnetic Resonance BiomolecularPharmacologychemistry.chemical_classificationconformationally definedChemistrypeptide librariesOrganic ChemistryGeneral MedicineNuclear magnetic resonance spectroscopyCombinatorial chemistryProtein Structure Tertiarypeptide designMolecular MedicinePeptidesdescription
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. Copyright (C) 2008 European Peptide Society and John Wiley & Sons. Ltd.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2008-01-01 | Journal of peptide science : an official publication of the European Peptide Society |