Covalent Linkage and Macrocylization Preserve and Enhance Synergistic Interactions in Catalytic Amyloids

Zsofia Lengyel-Zhand, Liam R. Marshall, Maximilian Jung, Megha Jayachandran, Min Chul Kim, Austin Kriews, Olga V. Makhlynets, H. Christopher Fry, Armin Geyer, Ivan V. Korendovych

Research output: Contribution to journalArticlepeer-review

Abstract

The self-assembly of short peptides into catalytic amyloid-like nanomaterials has proven to be a powerful tool in both understanding the evolution of early proteins and identifying new catalysts for practically useful chemical reactions. Here we demonstrate that both parallel and antiparallel arrangements of β-sheets can accommodate metal ions in catalytically productive coordination environments. Moreover, synergistic relationships, identified in catalytic amyloid mixtures, can be captured in macrocyclic and sheet-loop-sheet species, that offer faster rates of assembly and provide more complex asymmetric arrangements of functional groups, thus paving the way for future designs of amyloid-like catalytic proteins. Our findings show how initial catalytic activity in amyloid assemblies can be propagated and improved in more-complex molecules, providing another link in a complex evolutionary chain between short, potentially abiotically produced peptides and modern-day enzymes.

Original languageEnglish (US)
Pages (from-to)585-591
Number of pages7
JournalChemBioChem
Volume22
Issue number3
DOIs
StatePublished - Feb 2 2021

Keywords

  • amyloids
  • catalysis
  • peptides
  • self-assembly
  • synergistic interactions

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Organic Chemistry

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