Bacterial reaction centers purified with styrene maleic acid copolymer retain native membrane functional properties and display enhanced stability

Angew Chem Int Ed Engl. 2014 Oct 27;53(44):11803-7. doi: 10.1002/anie.201406412. Epub 2014 Sep 11.

Abstract

Integral membrane proteins often present daunting challenges for biophysical characterization, a fundamental issue being how to select a surfactant that will optimally preserve the individual structure and functional properties of a given membrane protein. Bacterial reaction centers offer a rare opportunity to compare the properties of an integral membrane protein in different artificial lipid/surfactant environments with those in the native bilayer. Here, we demonstrate that reaction centers purified using a styrene maleic acid copolymer remain associated with a complement of native lipids and do not display the modified functional properties that typically result from detergent solubilization. Direct comparisons show that reaction centers are more stable in this copolymer/lipid environment than in a detergent micelle or even in the native membrane, suggesting a promising new route to exploitation of such photovoltaic integral membrane proteins in device applications.

Keywords: detergents; membrane proteins; nanodiscs; reaction centers; styrene maleic acid.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Detergents / chemistry*
  • Maleates / chemistry*
  • Membrane Proteins / chemistry*

Substances

  • Detergents
  • Maleates
  • Membrane Proteins
  • maleic acid