Catalytic amyloids: Is misfolding folding?
Originally regarded as a disease symptom, amyloids have shown a rich diversity of functions, including biologically beneficial ones. As such, the traditional view of polypeptide aggregation into amyloid-like structures being ‘misfolding’ should rather be viewed as ‘alternative folding.’ Various amyl...
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Veröffentlicht in: | Current opinion in chemical biology 2021-10, Vol.64, p.145-153 |
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Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Originally regarded as a disease symptom, amyloids have shown a rich diversity of functions, including biologically beneficial ones. As such, the traditional view of polypeptide aggregation into amyloid-like structures being ‘misfolding’ should rather be viewed as ‘alternative folding.’ Various amyloid folds have been recently used to create highly efficient catalysts with specific catalytic efficiencies rivaling those of enzymes. Here we summarize recent developments and applications of catalytic amyloids, derived from both de novo and bioinspired designs, and discuss how progress in the last 2 years reflects on the field as a whole.
•Catalytic amyloids promote a variety of different chemical transformations with high efficiency.•Current approaches of catalytic amyloid design can be classified as de novo and bioinspired.•Catalytic amyloids can rely on cofactors or be cofactorless.•Traditional view of amyloid formation as misfolding is an oversimplification. |
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ISSN: | 1367-5931 1879-0402 |
DOI: | 10.1016/j.cbpa.2021.06.010 |