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Biophys J, September 2002, p. 1443-1454, Vol. 83, No. 3

and
*Institut de Biologie Physico-Chimique, Unité Mixte
de Recherche Centre National de la Recherche Scientifique 7099, Paris
75005 France; and
Institut Curie, Section de Recherche,
Unité Mixte de Recherche-Centre National de la Recherche
Scientifique 168 and Laboratoire de Recherche
Correspondant-Commissariat à l'Energie Nucléaire 8, 75231 Paris cedex, France
The 31P-nuclear magnetic resonance chemical
shift of phosphatidic acid in a membrane is sensitive to the lipid head
group packing and can report qualitatively on membrane lateral
compression near the aqueous interface. We have used high-resolution
31P-nuclear magnetic resonance to evaluate the lateral
compression on each side of asymmetrical lipid vesicles. When
monooleoylphosphatidylcholine was added to the external monolayer of
sonicated vesicles containing dioleoylphosphatidylcholine and
dioleoylphosphatidic acid, the variation of 31P chemical
shift of phosphatidic acid indicated a lateral compression in the
external monolayer. Simultaneously, a slight dilation was observed in
the inner monolayer. In large unilamellar vesicles on the other hand
the lateral pressure increased in both monolayers after asymmetrical
insertion of monooleoylphosphatidylcholine. This can be explained by
assuming that when monooleoylphosphatidylcholine is added to large
unilamellar vesicles, the membrane bends until the strain is the same
in both monolayers. In the case of sonicated vesicles, a change of
curvature is not possible, and therefore differential packing in the
two layers remains. We infer that a variation of lipid asymmetry by
generating a lateral strain in the membrane can be a physiological way
of modulating the conformation of membrane proteins.
Biophys J, September 2002, p. 1443-1454, Vol. 83, No. 3
© 2002 by the Biophysical Society 0006-3495/02/09/1443/12 $2.00
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