Synthetic β-Barrel by Metal-Induced Folding and Assembly

J Am Chem Soc. 2018 Jul 18;140(28):8644-8647. doi: 10.1021/jacs.8b04284. Epub 2018 Jul 9.


The de novo construction of repeat proteins has received much attention from biologists and chemists, yet that of a β-barrel structure, one of the most well-known classes, has not been accomplished to date. Here, we report the first chemical construction of a β-barrel tertiary structure with a pore through a combination of peptide folding and metal-directed self-assembly. Coordination of zinc salts to an eight-residue peptide fragment bearing β-strand- and loop-forming sequences resulted in a β-barrel in which six-stranded cylindrical antiparallel β-sheets formed a hydrophobic pore with a specific shape.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Hydrophobic and Hydrophilic Interactions
  • Macrocyclic Compounds / chemistry*
  • Models, Molecular
  • Peptides / chemistry*
  • Porosity
  • Protein Conformation, beta-Strand*
  • Protein Folding
  • Protein Structure, Tertiary
  • Zinc / chemistry*


  • Macrocyclic Compounds
  • Peptides
  • Zinc