The Promiscuity of [beta]-Strand Pairing Allows for Rational Design of [beta]-Sheet Face Inversion
- UC
Recent studies suggest the dominant role of main-chain H-bond formation in specifying {beta}-sheet topology. Its essentially sequence-independent nature implies a large degree of freedom in designing {beta}-sheet-based nanomaterials. Here we show rational design of {beta}-sheet face inversions by incremental deletions of {beta}-strands from the single-layer {beta}-sheet of Borrelia outer surface protein A. We show that a {beta}-sheet structure can be maintained when a large number of native contacts are removed and that one can design large-scale conformational transitions of a {beta}-sheet such as face inversion by exploiting the promiscuity of strand-strand interactions. High-resolution X-ray crystal structures confirmed the success of the design and supported the importance of main-chain H-bonds in determining {beta}-sheet topology. This work suggests a simple but effective strategy for designing and controlling nanomaterials based on {beta}-rich peptide self-assemblies.
- Research Organization:
- Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
- Sponsoring Organization:
- USDOE
- OSTI ID:
- 1007089
- Journal Information:
- J. Am. Chem. Soc., Journal Name: J. Am. Chem. Soc. Journal Issue: (44) ; 11, 2008 Vol. 130; ISSN JACSAT; ISSN 0002-7863
- Country of Publication:
- United States
- Language:
- ENGLISH
Similar Records
Factors contributing to decreased protein stability when aspartic acid residues are in {beta}-sheet regions.
Solid-state NMR analysis of the {beta}-strand orientation of the protofibrils of amyloid {beta}-protein