| Literature DB >> 11841829 |
Noboru Ishiyama1, Christopher M Hill, Ian R Bates, George Harauz.
Abstract
Binary lipid monolayers consisting of equimolar proportions of a phosphoinositide and a nickel-chelating lipid formed helical tubular vesicular structures, which appeared to be induced and/or stabilized by myelin basic protein (MBP). Another basic polypeptide, poly-L-lysine, had a similar effect but not to as great a degree as MBP; the proteins thus appeared to act as polycations. Although, the nickel-chelating lipid is a synthetic product, other endogenous divalent cations such as Zn(2+), as well as phosphoinositides, are integral and dynamic components of the myelin sheath in vivo. There, comparable helical tubular structures might represent a means for sequestration of these lipids into domains of high local concentration, perhaps in regions where the membrane is greatly curved.Entities:
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Year: 2002 PMID: 11841829 DOI: 10.1016/s0009-3084(02)00002-6
Source DB: PubMed Journal: Chem Phys Lipids ISSN: 0009-3084 Impact factor: 3.329