Semi-Rationally Designed Short Peptides Self-Assemble and Bind Hemin to Promote Cyclopropanation

Oleksii Zozulia, Ivan V. Korendovych

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

The self-assembly of short peptides gives rise to versatile nanoassemblies capable of promoting efficient catalysis. We have semi-rationally designed a series of seven-residue peptides that form hemin-binding catalytic amyloids to facilitate enantioselective cyclopropanation with efficiencies that rival those of engineered hemin proteins. These results demonstrate that: 1) Catalytic amyloids can bind complex metallocofactors to promote practically important multisubstrate transformations. 2) Even essentially flat surfaces of amyloid assemblies can impart a substantial degree of enantioselectivity without the need for extensive optimization. 3) The ease of peptide preparation allows for straightforward incorporation of unnatural amino acids and the preparation of peptides made from d-amino acids with complete reversal of enantioselectivity.

Original languageEnglish (US)
Pages (from-to)8108-8112
Number of pages5
JournalAngewandte Chemie - International Edition
Volume59
Issue number21
DOIs
StatePublished - May 18 2020

Keywords

  • amyloids
  • cyclopropanation
  • hemin
  • peptides
  • self-assembly

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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