Spontaneously forming ellipsoidal phospholipid unilamellar vesicles and their interactions with helical domains of saposin C

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DOIResolve DOI: http://doi.org/10.1021/la062275j
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TypeArticle
Journal titleLangmuir
ISSN07437463
Volume22
Issue26
Pages1102833; # of pages: 10996
SubjectAnimals; Phospholipids; Protein Structure, Secondary; Protein Structure, Tertiary; Saposins; Unilamellar Liposomes
AbstractWe have observed a bimodal distribution of ellipsoidal unilamellar vesicles (ULVs) in a phospholipid mixture composed of dioleoyl phosphatidylserine (DOPS) and dipalmitoyl and dihexanoyl phosphatidylcholine, DPPC and DHPC, respectively. Dynamic light scattering and transmission electron microscopy data indicate a bimodal size distribution of these nanoparticles with hydrodynamic radii of approximately 200 and >500 nm, while small-angle neutron scattering data were fit using a model of coexisting monodisperse morphologies, namely, oblate and triaxial ellipsoidal vesicles. Unlike DOPS ULV formed by sonication, which can fuse days after being formed, these ULVs are stable over a period of 12 months at 4 degrees C. We also report on the structure of these ULVs associated with the two helical peptide domains (H1 and H2) of a glucosylprotein, namely, Saposin C, to gain some insight into protein-membrane interactions.
Publication date
AffiliationNational Research Council Canada; NRC Canadian Neutron Beam Centre
Peer reviewedNo
Identifier10367391
NPARC number12328234
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Record identifieredc48d6b-fc2c-446a-af6c-8a181576453c
Record created2009-09-10
Record modified2016-05-09
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