Abstract

The protein-only infectious agents known as prions exist within cellular matrices as populations of assembled polypeptide phases ranging from particles to amyloid fibres. These phases appear to undergo Darwinian-like selection and propagation, yet remarkably little is known about their accessible chemical and biological functions. Here we construct simple peptides that assemble into well-defined amyloid phases and define paracrystalline surfaces able to catalyse specific enantioselective chemical reactions. Structural adjustments of individual amino acid residues predictably control both the assembled crystalline order and their accessible catalytic repertoire. Notably, the density and proximity of the extended arrays of enantioselective catalytic sites achieve template-directed polymerization of new polymers. These diverse amyloid templates can now be extended as dynamic self-propagating templates for the construction of even more complex functional materials.

  • Compound

    4-hydroxy-4-(6-methoxy-2-naphthyl)-2-butanone

  • Compound

    (R)-4-hydroxy-4-(6-methoxynaphthalen-2-yl)butan-2-one

  • Compound

    (S)-4-hydroxy-4-(6-methoxynaphthalen-2-yl)butan-2-one

  • Compound

    1-(6-methoxy-2-naphthalenyl)-1,3-butanedione

  • Compound

    6-(tert-butoxymethyl)naphthalen-2-amine

  • Compound

    6-(N,N-dimethylamino)-2-naphthaldehyde

  • Compound

    6-amino-2-naphthaldehyde

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Acknowledgements

We are grateful to J. Taylor and H. Yi in the Emory Robert P. Apkarian Microscopy Core for TEM advice and training. This work was supported initially by the McDonnell Foundation, transiently by NSF and the NASA Astrobiology Program, under the NSF Center for Chemical Evolution, CHE-1004570, and then predominantly funded by Emory University, The Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences of the US Department of Energy through Grant DE-ER15377 for peptide synthesis and assembly characterization, and NSF CHE-1507932 for personnel, supplies, equipment, and structural characterization support.

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Affiliations

  1. Departments of Chemistry and Biology, Emory University, Atlanta, Georgia 30322, USA

    • Tolulope O. Omosun
    • , W. Seth Childers
    • , Dibyendu Das
    • , Anil K. Mehta
    • , Ting Pan
    •  & David G. Lynn
  2. School of Chemical Engineering, Georgia Institute of Technology, Atlanta, Georgia 30332, USA

    • Ming-Chien Hsieh
    •  & Martha A. Grover
  3. Department of Physics, Emory University, Atlanta, Georgia 30322, USA

    • Neil R. Anthony
    •  & Keith M. Berland

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All authors contributed significantly to the design of experiments, analysing the data and drafting of the manuscript.

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The authors declare no competing financial interests.

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Correspondence to David G. Lynn.

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DOI

https://doi.org/10.1038/nchem.2738

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