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Originally published as Biophys J. BioFAST on August 31, 2004.
doi:10.1529/biophysj.104.046169
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Biophysical Journal 87:3213-3220 (2004)
© 2004 The Biophysical Society

The Protein-Tethered Lipid Bilayer: A Novel Mimic of the Biological Membrane

Frank Giess *, Marcel G. Friedrich *, Joachim Heberle {dagger}, Renate L. Naumann * and Wolfgang Knoll *

* Max Planck Institute for Polymer Research, Mainz, Germany; and {dagger} Research Centre Juelich, Juelich, Germany

Correspondence: Address reprint requests to Renate L. Naumann, E-mail: naumannr{at}mpip-mainz.mpg.de.

A new concept of solid-supported tethered bilayer lipid membrane (tBLM) for the functional incorporation of membrane proteins is introduced. The incorporated protein itself acts as the tethering molecule resulting in a versatile system in which the protein determines the characteristics of the submembraneous space. This architecture is achieved through a metal chelating surface, to which histidine-tagged (His-tagged) membrane proteins are able to bind in a reversible manner. The tethered bilayer lipid membrane is generated by substitution of protein-bound detergent molecules with lipids using in-situ dialysis or adsorption. The system is characterized by surface plasmon resonance, quartz crystal microbalance, and electrochemical impedance spectroscopy. His-tagged cytochrome c oxidase (CcO) is used as a model protein in this study. However, the new system should be applicable to all recombinant membrane proteins bearing a terminal His-tag. In particular, combination of surface immobilization and membrane reconstitution opens new prospects for the investigation of functional membrane proteins by various surface-sensitive techniques under a defined electric field.




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