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* Department of Chemistry, the Institute for Biophysical Dynamics and the James Franck Institute, the University of Chicago, Chicago, Illinois;
Manuel Lujan Jr. Neutron Scattering Center, Los Alamos National Laboratory, Los Alamos, New Mexico; and
Materials Research Department, Risø National Laboratory, Roskilde, Denmark
Correspondence: Address reprint requests to Ka Yee C. Lee, Dept. of Chemistry, the Institute for Biophysical Dynamics and the James Franck Institute, the University of Chicago, 5735 S. Ellis Ave., Chicago, IL 60637. E-mail: kayeelee{at}uchicago.edu.
The mechanism by which poloxamer 188 (P188) seals a damaged cell membrane is examined using the lipid monolayer as a model system. X-ray reflectivity and grazing-incidence x-ray diffraction results show that at low nominal lipid density, P188, by physically occupying the available area and phase separating from the lipids, forces the lipid molecules to pack tightly and restore the barrier function of the membrane. Upon compression to bilayer equivalent pressure, P188 is squeezed out from the lipid monolayer, allowing a graceful exit of P188 when the membrane integrity is restored.
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