期刊
NATURE CHEMISTRY
卷 6, 期 4, 页码 303-309出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEM.1894
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资金
- National Institutes of Health [GM54616]
- National Science Foundation (NSF) Emerging Frontiers in Research and Innovation (EFRI) program [1332349]
- Oak Ridge Associated Universities Ralph E. Powe Junior Faculty Enhancement award
- Materials Research Science and Engineering Center programme of the NSF [DMR-1120901]
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.
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