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PMID: 15701521 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Lipid rafts have different sizes depending on membrane composition: a time-resolved fluorescence resonance energy transfer study.

Journal of molecular biology ·Vol. 346 ·No. 4 ·2005-03-04 ·Pages 1109-20

de Almeida RF, Loura LM, Fedorov A, Prieto M

Abstract

The ternary lipid system palmitoylsphingomyelin (PSM)/palmitoyloleoylphosphatidylcholine (POPC)/cholesterol is a model for lipid rafts. Previously the phase diagram for that mixture was obtained, establishing the composition and boundaries for lipid rafts. In the present work, this system is further studied in order to characterize the size of the rafts. For this purpose, a time-resolved fluorescence resonance energy transfer (FRET) methodology, previously applied with success to a well-characterized phosphatidylcholine/cholesterol binary system, is used. It is concluded that: (1) the rafts on the low raft fraction of the raft region are small (below 20 nm), whereas on the other side the domains are larger; (2) on the large domain region, the domains reach larger sizes in the ternary system (> approximately 75-100 nm) than in binary systems phosphatidylcholine/cholesterol (between approximately 20 and approximately 75-100 nm); (3) the raft marker ganglioside G(M1) in small amounts (and excess cholera toxin subunit B) does not affect the general phase behaviour of the lipid system, but can increase the size of the rafts on the small to intermediate domain region. In summary, lipid-lipid interactions alone can originate lipid rafts on very different length scales. The conclusions presented here are consistent with the literature concerning both model systems and cell membrane studies.

MeSH Terms
Cholesterol/chemistry Fluorescence Resonance Energy Transfer Membrane Microdomains/chemistry Phosphatidylcholines/chemistry Sphingomyelins/chemistry Temperature Time Factors
Chemicals
Phosphatidylcholines Sphingomyelins palmitoylsphingomyelin Cholesterol
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
de Almeida Rodrigo F M
Centro de Química-Física Molecular, Instituto Superior Técnico, Universidade Técnica de Lisboa, Lisboa, Portugal. [email protected]
Loura Luís M S
Fedorov Alexander
Prieto Manuel
Article Info
Journal
Journal of molecular biology
Abbr.
J Mol Biol
ISSN
0022-2836
Published
2005-03-04
Epub
2005-00-12
Pages
1109-20
Language
English
Region
England
NLM ID
2985088R
Subset
IM
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