Document Detail

Membrane resistance to Triton X-100 explored by real-time atomic force microscopy.
MedLine Citation:
PMID:  16768509     Owner:  NLM     Status:  MEDLINE    
Lateral segregation of lipids and proteins in biological membranes leads to the formation of detergent-resistant domains, also called "rafts". Understanding the mechanisms governing the biomembrane's resistance to solubilization by detergents is crucial in biochemical research. Here, we used real-time atomic force microscopy (AFM) imaging to visualize the behavior of a model supported lipid bilayer in the presence of different Triton X-100 (TX-100) concentrations. Mixed dioleoylphosphatidylcholine/dipalmitoylphosphatidylcholine (DOPC/DPPC) supported bilayers were prepared by vesicle fusion. Real-time AFM imaging revealed that, at concentrations below the critical micelle concentration (CMC), TX-100 did not solubilize the bilayer, but the DPPC domains were eroded in a time-dependent manner. This effect was attributed to the DPPC molecular packing disorganization by the detergent starting from the DOPC/DPPC interface. Just above the CMC, the detergent led to a complete solubilization of the DOPC matrix, leaving the DPPC domains unaltered. At higher TX-100 concentrations, the DOPC was also immediately removed just after detergent addition, and the DPPC domains remaining on the mica surface appeared to be more swollen and were gradually solubilized. This progressive solubilization of the DPPC remaining phase did not start at the edge of the domains but from holes appearing and expanding at the center of DPPC patches. The swelling of the DPPC domains was directly correlated with TX-100 concentration above the CMC and with detergent intercalation between DPPC molecules. We are convinced that this approach will provide a key system to elucidate the physical mechanisms of membrane solubilization by nonionic detergents.
Sandrine Morandat; Karim El Kirat
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Langmuir : the ACS journal of surfaces and colloids     Volume:  22     ISSN:  0743-7463     ISO Abbreviation:  Langmuir     Publication Date:  2006 Jun 
Date Detail:
Created Date:  2006-06-13     Completed Date:  2007-07-20     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9882736     Medline TA:  Langmuir     Country:  United States    
Other Details:
Languages:  eng     Pagination:  5786-91     Citation Subset:  IM    
Laboratoire de Génie Enzymatique et Cellulaire, Université de Technologie de Compiègne, UMR-CNRS 6022, BP 20529, 60205 Compiègne Cedex, France.
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MeSH Terms
1,2-Dipalmitoylphosphatidylcholine / chemistry
Detergents / chemistry*
Lipid Bilayers / chemistry
Membrane Lipids / isolation & purification
Membrane Proteins / isolation & purification*
Microscopy, Atomic Force
Models, Molecular
Octoxynol / chemistry*
Phosphatidylcholines / chemistry
Reg. No./Substance:
0/Detergents; 0/Gels; 0/Lipid Bilayers; 0/Membrane Lipids; 0/Membrane Proteins; 0/Micelles; 0/Phosphatidylcholines; 10015-85-7/1,2-oleoylphosphatidylcholine; 2644-64-6/1,2-Dipalmitoylphosphatidylcholine; 9002-93-1/Octoxynol

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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