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Nat Chem. 2014 Apr;6(4):303-9. doi: 10.1038/nchem.1894. Epub 2014 Mar 16.

Short peptides self-assemble to produce catalytic amyloids.

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1] Department of Chemistry, Syracuse University, Syracuse, New York 13244, USA [2].
Institute for Neurodegenerative Diseases and Department of Neurology, University of California - San Francisco, San Francisco, California 94143, USA.
Department of Chemistry, Syracuse University, Syracuse, New York 13244, USA.
Department of Pharmaceutical Chemistry, University of California - San Francisco, Francisco, California 94158, USA.


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 Zn(2+)-dependent esterases. Zn(2+) 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.

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