Biointerphases

Journal for Biophysical Chemistry

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Open Access

Protein tethered lipid bilayer: An alternative mimic of the biological membrane (Mini Review)

  • Renate L. C. Naumann1 and
  • Wolfgang Knoll1
Biointerphases3:30200101

https://doi.org/10.1116/1.2936939

Received: 23 January 2008

Accepted: 11 July 2008

Abstract

An overview is given about results obtained so far with an alternative concept of solid-supported tethered lipid bilayers for the functional incorporation of membrane proteins. The incorporated protein itself acts as the tethering molecule resulting in a versatile system where the protein determines the characteristics of submembraneous space. This architecture is achieved through a metal chelating surface, onto which histidine-tagged (his-tagged) membrane proteins are able to bind in a reversible manner. The tethered bilayer membrane is generated by substitution of protein bund detergent molecules with lipids using in situ dialysis or adsorption. Histidine-tagged ctochrome c oxidase is used as a model protein in this study. However, the system should be applicable to all recombinant membrane proteins bearing a terminal his tag. The system is particularly designed, among other surface-analytical techniques, for a combined application of electrochemical and vibrational spectroscopy measurements.

Authors’ Affiliations

(1)
Max Planck Institute for Polymer Research

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© American Vacuum Society 2008