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Biophys J, October 2000, p. 2066-2074, Vol. 79, No. 4
Division of Biochemistry and Molecular Biology, School of Biological Sciences, University of Southampton, Southampton SO16 7PX, United Kingdom
The outer membrane porin OmpF from Escherichia
coli has been reconstituted into lipid bilayers of defined
composition, and fluorescence spectroscopy is used to characterize its
interaction with the surrounding lipid. OmpF is a trimer within the
membrane. It contains two Trp residues per monomer, Trp214
at the lipid-protein interface and Trp61 at the trimer
interface. The fluorescence of Trp-214 in the mutant W61F is quenched
by dibromostearoylphosphatidylcholine (di(Br2C18:0)PC), whereas the fluorescence of Trp61 in the mutant W214F is
not quenched by di(Br2C18:0)PC when fluorescence is excited
directly through the Trp rather than through the Tyr residues.
Measurements of relative fluorescence quenching for OmpF reconstituted
into mixtures of lipid X and di(Br2C18:0)PC have been
analyzed to give the binding constant of lipid X for OmpF, relative to
that for dioleoylphosphatidylcholine (di(C18:1)PC). The
phosphatidylcholine showing the strongest binding to OmpF is
dimyristoyloleoylphosphatidylcholine (di(C14:1)PC) with binding constants decreasing with either increasing or decreasing fatty acyl
chain length. Comparison with various theories for hydrophobic matching
between lipids and proteins suggests that in the chain length range
from C14 to C20, hydrophobic matching is achieved largely by distortion
of the lipid bilayer around the OmpF, whereas for chains longer than
C20, distortion of both the lipid bilayer and of the protein is
required to achieve hydrophobic matching. Phosphatidylcholine and
phosphatidylethanolamine bind with equal affinity to OmpF, but the
affinity for phosphatidylglycerol is about half that for phosphatidylcholine.
Biophys J, October 2000, p. 2066-2074, Vol. 79, No. 4
© 2000 by the Biophysical Society 0006-3495/00/10/2066/09 $2.00
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