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American Chemical Society, Langmuir, 26(22), p. 11028-11033, 2006

DOI: 10.1021/la062275j

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

Journal article published in 2006 by Mu-Ping Nieh ORCID, Jeremy Pencer, John Katsaras, Xiaoyang Qi
This paper is available in a repository.
This paper is available in a repository.

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Abstract

We 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. ; system details: machine converted author identifier PE to PID, February 2012