Cover Picture: Enhancing β3-Peptide Bundle Stability by Design (ChemBioChem 7/2011)

Authors

  • Cody J. Craig,

    1. Department of Chemistry, Yale University, 225 Prospect Street, New Haven, CT 06520-8107 (USA)
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  • Dr. Jessica L. Goodman,

    1. Department of Chemistry, Yale University, 225 Prospect Street, New Haven, CT 06520-8107 (USA)
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  • Prof. Alanna Schepartz

    Corresponding author
    1. Departments of Chemistry and Molecular, Cellular and Developmental Biology, Yale University, 225 Prospect Street, New Haven, CT 06520-8107 (USA), Fax: (+1) 203-432-3486
    • Departments of Chemistry and Molecular, Cellular and Developmental Biology, Yale University, 225 Prospect Street, New Haven, CT 06520-8107 (USA), Fax: (+1) 203-432-3486
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Abstract

original image

The cover picture shows the structure of a β-peptide bundle protein whose stability was improved by optimizing salt-bridge interactions on the bundle surface. There is considerable current interest in the design of higher-order, non-proteinaceous assemblies possessing defined oligomeric states, as these have potential as nanomaterials and catalysts. We reported previously that certain β3-peptides self-assemble spontaneously in aqueous solution into discrete bundles of defined stoichiometry (β-peptide bundles) whose kinetic and thermodynamic metrics are virtually indistinguishable from those of natural proteins. Here we show that the stability of a β-peptide bundle can be tuned by controlling the length of a solvent-exposed surface salt-bridge interaction. Combined with previous work on the roles of internal packing residues, these results provide another critical step in the bottom-up assembly of β-peptides with defined sizes, reproducible structures, and sophisticated function. For more information see the paper by A. Schepartz, et al. on p. 1035 ff.

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