Short peptides self-assemble to produce catalytic amyloids

Caroline M. Rufo, Yurii S. Moroz, Olesia V. Moroz, Jan Stöhr, Tyler A. Smith, Xiaozhen Hu, William F. Degrado, Ivan V. Korendovych

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217 Scopus citations

Abstract

Enzymes fold into unique three-dimensional structures, which underlie their remarkable catalytic properties. The requirement to adopt a stable, folded conformation is likely to contribute to their relatively large size (>10,000 Da). However, much shorter peptides can achieve well-defined conformations through the formation of amyloid fibrils. To test whether short amyloid-forming peptides might in fact be capable of enzyme-like catalysis, we designed a series of seven-residue peptides that act as Zn2+ -dependent esterases. Zn2+ helps stabilize the fibril formation, while also acting as a cofactor to catalyse acyl ester hydrolysis. These results indicate that prion-like fibrils are able to not only catalyse their own formation, but they can also catalyse chemical reactions. Thus, they might have served as intermediates in the evolution of modern-day enzymes. These results also have implications for the design of self-assembling nanostructured catalysts including ones containing a variety of biological and non-biological metal ions.

Original languageEnglish (US)
Pages (from-to)303-309
Number of pages7
JournalNature Chemistry
Volume6
Issue number4
DOIs
StatePublished - Apr 2014

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ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

Cite this

Rufo, C. M., Moroz, Y. S., Moroz, O. V., Stöhr, J., Smith, T. A., Hu, X., Degrado, W. F., & Korendovych, I. V. (2014). Short peptides self-assemble to produce catalytic amyloids. Nature Chemistry, 6(4), 303-309. https://doi.org/10.1038/nchem.1894