Catalytic amyloids: Is misfolding folding?

Liam R. Marshall, Ivan V. Korendovych

Research output: Contribution to journalReview articlepeer-review

Abstract

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.

Original languageEnglish (US)
Pages (from-to)145-153
Number of pages9
JournalCurrent Opinion in Chemical Biology
Volume64
DOIs
StatePublished - Oct 2021

Keywords

  • Amyloid
  • Catalysis
  • Peptide
  • Self-assembly

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry

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