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Article: Detection and characterization of laterally phase separated cholesterol domains in model lipid membranes

TitleDetection and characterization of laterally phase separated cholesterol domains in model lipid membranes
Authors
KeywordsBilayer
Cholesterol
DMPC
Domains
Liquid-ordered
Issue Date2003
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/colsurfb
Citation
Colloids And Surfaces B: Biointerfaces, 2003, v. 29 n. 2-3, p. 217-231 How to Cite?
AbstractWe present evidence that laterally phase separated cholesterol domains constitute a new, equilibrium phase in biological membranes. The domains are characterized in multi-lamellar vesicles (MLV) made of cholesterol and dimyristoylphosphatidylcholine (DMPC) but are also shown to exist in biologically relevant, egg lecithin systems containing a mixture of phospholipids. This work utilizes the fluorescent membrane probes 1-acyl-2-[12-[(5-dimethylamino-1-naphthalenesufonyl)amino]dodecanoyl]-sn- glycero-3-phosphocholine (DANSYL), and ergosta-5,7,9(11),22-tetraen-3β-ol (ERGO), which have been shown to be minimally invasive mimics of native membrane lipids. The highlight of the work is a heating-induced alleviation of a DANSYL blue shift at relatively high (but undersaturated) cholesterol loadings, which is reversible through at least three heating and cooling cycles. Comparison of the DANSYL spectral shifts with published DMPC-cholesterol phase diagrams shows unequivocally that the spectral results cannot be explained in terms of previously understood phase behavior. Rather, a lateral phase separation occurs within the vesicle bilayer, giving rise to cholesterol micro-domains. The cholesterol domains appear to coexist with, and should not be confused with, the well-known liquid-order phase that arises because of the cholesterol condensation effect. Additional studies involving ERGO-DANSYL energy transfer show a sequestration of probes within the bilayer, confirming the DANSYL spectral data, and a model that includes domains provides the best description of measured energy transfer efficiencies. Best fits of the energy transfer data, using a mathematical model developed to account for the presence of domains, indicates the domain size to be in the range 10-20 nm. © 2003 Elsevier Science B.V. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/92482
ISSN
2015 Impact Factor: 3.902
2015 SCImago Journal Rankings: 1.105
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorTroup, GMen_HK
dc.contributor.authorTulenko, TNen_HK
dc.contributor.authorLee, SPen_HK
dc.contributor.authorWrenn, SPen_HK
dc.date.accessioned2010-09-17T10:47:36Z-
dc.date.available2010-09-17T10:47:36Z-
dc.date.issued2003en_HK
dc.identifier.citationColloids And Surfaces B: Biointerfaces, 2003, v. 29 n. 2-3, p. 217-231en_HK
dc.identifier.issn0927-7765en_HK
dc.identifier.urihttp://hdl.handle.net/10722/92482-
dc.description.abstractWe present evidence that laterally phase separated cholesterol domains constitute a new, equilibrium phase in biological membranes. The domains are characterized in multi-lamellar vesicles (MLV) made of cholesterol and dimyristoylphosphatidylcholine (DMPC) but are also shown to exist in biologically relevant, egg lecithin systems containing a mixture of phospholipids. This work utilizes the fluorescent membrane probes 1-acyl-2-[12-[(5-dimethylamino-1-naphthalenesufonyl)amino]dodecanoyl]-sn- glycero-3-phosphocholine (DANSYL), and ergosta-5,7,9(11),22-tetraen-3β-ol (ERGO), which have been shown to be minimally invasive mimics of native membrane lipids. The highlight of the work is a heating-induced alleviation of a DANSYL blue shift at relatively high (but undersaturated) cholesterol loadings, which is reversible through at least three heating and cooling cycles. Comparison of the DANSYL spectral shifts with published DMPC-cholesterol phase diagrams shows unequivocally that the spectral results cannot be explained in terms of previously understood phase behavior. Rather, a lateral phase separation occurs within the vesicle bilayer, giving rise to cholesterol micro-domains. The cholesterol domains appear to coexist with, and should not be confused with, the well-known liquid-order phase that arises because of the cholesterol condensation effect. Additional studies involving ERGO-DANSYL energy transfer show a sequestration of probes within the bilayer, confirming the DANSYL spectral data, and a model that includes domains provides the best description of measured energy transfer efficiencies. Best fits of the energy transfer data, using a mathematical model developed to account for the presence of domains, indicates the domain size to be in the range 10-20 nm. © 2003 Elsevier Science B.V. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/colsurfben_HK
dc.relation.ispartofColloids and Surfaces B: Biointerfacesen_HK
dc.subjectBilayeren_HK
dc.subjectCholesterolen_HK
dc.subjectDMPCen_HK
dc.subjectDomainsen_HK
dc.subjectLiquid-ordereden_HK
dc.titleDetection and characterization of laterally phase separated cholesterol domains in model lipid membranesen_HK
dc.typeArticleen_HK
dc.identifier.emailLee, SP: sumlee@hku.hken_HK
dc.identifier.authorityLee, SP=rp01351en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/S0927-7765(03)00020-1en_HK
dc.identifier.scopuseid_2-s2.0-0038406406en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0038406406&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume29en_HK
dc.identifier.issue2-3en_HK
dc.identifier.spage217en_HK
dc.identifier.epage231en_HK
dc.identifier.isiWOS:000183004800016-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridTroup, GM=7005997903en_HK
dc.identifier.scopusauthoridTulenko, TN=7005077545en_HK
dc.identifier.scopusauthoridLee, SP=7601417497en_HK
dc.identifier.scopusauthoridWrenn, SP=6603940041en_HK

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