Phospholipid/protein cones.
The presence of protein in tubule-forming solutions of the diacetylenic phospholipid 1,2-bis(10,12-tricosadiynoyl)-sn-glycero-3-phosphocholine results in the formation of hollow cones rather than the expected hollow cylinders. Differential phase-contrast video microscopy reveals that cones grow from proteinaceous nodules in a fashion similar to cylindrical tubule growth from spherical vesicles. Spatially resolved electron-beam energy-dispersive X-ray fluorescence spectroscopy shows the protein to be associated with the cone wall. Small-angle X-ray scattering shows that, like the protein-free cylinders, the cones are multilamellar with essentially identical interlamellar spacing.
Mishra
Bijaya K
BK
Department of Chemistry, Louisiana State University, Baton Rouge, Louisiana 70808, USA.
Thomas
Britt N
BN
D053280:Diynes; D018625:Microscopy, Atomic Force; D008855:Microscopy, Electron, Scanning; D009113:Muramidase / Q000737:chemistry*; D010713:Phosphatidylcholines / Q000737:chemistry*; D010743:Phospholipids / Q000737:chemistry*; D010767:Phosphorylcholine / Q000031:analogs & derivatives* / Q000737:chemistry; D012542:Scattering, Radiation; D014965:X-Rays
D053280:Diynes; D010713:Phosphatidylcholines; D010743:Phospholipids; D010767:Phosphorylcholine; C053923:1,2-bis(10,12-tricosadiynoyl)phosphatidylcholine; D009113:Muramidase