Crown ethers are small, cyclic polyethers that have found wide-spread use in phase-transfer catalysis and, to a certain degree, in protein chemistry. Crown ethers readily bind metallic and organic cations, including positively charged amino acid side chains. We elucidated the crystal structures of several protein-crown ether co-crystals grown in the presence of 18-crown-6. We then employed biophysical methods and molecular dynamics simulations to compare these complexes with the corresponding apoproteins and with similar complexes with ring-shaped low-molecular-weight polyethylene glycols. Our studies show that crown ethers can modify protein surface behavior dramatically by stabilizing either intra- or intermolecular interactions. Consequently, we propose that crown ethers can be used to modulate a wide variety of protein surface behaviors, such as oligomerization, domain-domain interactions, stabilization in organic solvents, and crystallization.

Original languageEnglish
Pages (from-to)13054-13058
Number of pages5
JournalAngewandte Chemie - International Edition
Issue number48
Publication statusPublished - Nov 24 2014


  • Crown compounds
  • Crystal growth
  • Molecular dynamics
  • Protein engineering
  • Protein surfaces

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis


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