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Phospholipid/protein cones.

Bijaya K Mishra1, Britt N Thomas

  • 1Department of Chemistry, Louisiana State University, Baton Rouge, Louisiana 70808, USA.

Journal of the American Chemical Society
|June 13, 2002
PubMed
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Protein in diacetylenic phospholipid solutions unexpectedly forms hollow cones, not cylinders. These cones grow from protein nodules, similar to cylinder formation, and possess multilamellar structures.

Area of Science:

  • Biomaterials Science
  • Materials Chemistry
  • Structural Biology

Background:

  • Diacetylenic phospholipids self-assemble into tubular structures.
  • Protein interactions can influence self-assembly processes.
  • Understanding protein-lipid interactions is crucial for biomaterial design.

Purpose of the Study:

  • To investigate the effect of protein presence on the self-assembly of a specific diacetylenic phospholipid.
  • To characterize the morphology and structure of the resulting self-assembled structures.
  • To elucidate the role of protein in the tubule formation process.

Main Methods:

  • Differential phase-contrast video microscopy for observing growth dynamics.
  • Electron-beam energy-dispersive X-ray fluorescence spectroscopy for elemental analysis.

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  • Small-angle X-ray scattering for structural characterization.

    • Main Results:

    • Protein presence altered the morphology from expected hollow cylinders to hollow cones.
    • Cone formation initiated from proteinaceous nodules.
    • Protein was localized within the cone walls.
    • The cones exhibited multilamellar structures with consistent interlamellar spacing.

    Conclusions:

    • Proteins can significantly alter the self-assembly pathways of diacetylenic phospholipids.
    • Protein-induced morphological changes are driven by specific interactions at the assembly interface.
    • The resulting protein-associated structures retain key structural features like multilamellarity.