Fluorination in the design of membrane protein assemblies

Methods Mol Biol. 2013:1063:227-43. doi: 10.1007/978-1-62703-583-5_13.


Protein design approaches based on the binary patterning of nonpolar and polar amino acids have been successful in generating native-like protein structures of amphiphilic α-helices or idealized amphiphilic β-strands in aqueous solution. Such patterning is not possible in the nonpolar environment of biological membranes, precluding the application of conventional approaches to the design of membrane proteins that assemble into discrete aggregates. This review surveys a promising, new strategy for membrane protein design that exploits the unique properties of fluorocarbons-in particular, their ability to phase separate from both water (due to their hydrophobicity) and hydrocarbons (due to their lipophobicity)-to generate membrane protein assemblies. The ability to design such discrete assemblies should enable the disruption of protein-protein interactions and provide templates for novel biomaterials and therapeutics.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Drug Design*
  • Halogenation*
  • Humans
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism*
  • Molecular Sequence Data
  • Protein Stability
  • Protein Structure, Secondary


  • Membrane Proteins