Fluorination in the Design of Membrane Protein Assemblies

  • Vijay M. Krishnamurthy
  • Krishna Kumar
Part of the Methods in Molecular Biology book series (MIMB, volume 1063)


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.

Key words

Fluorine Fluorocarbon Membrane Aggregate Oligomer Assembly Coiled coil Alpha-helix Beta-sheet Antimicrobial peptide 


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Copyright information

© Springer Science+Business Media, LLC 2013

Authors and Affiliations

  • Vijay M. Krishnamurthy
    • 1
  • Krishna Kumar
    • 1
    • 2
  1. 1.Department of ChemistryTufts UniversityMedfordUSA
  2. 2.Cancer Center, Tufts Medical CenterBostonUSA

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