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Supported phospholipid bilayers for two-dimensional protein crystallization.

E E Uzgiris

    Biochemical and Biophysical Research Communications
    |January 29, 1986
    PubMed
    Summary
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    Supported phospholipid bilayers on electron microscope grids promote uniform 2D crystal growth of antibodies. This method achieves high surface coverage, ideal for studying antibody-antigen interactions under specific binding conditions.

    Area of Science:

    • Biophysics
    • Materials Science
    • Immunology

    Background:

    • Phospholipid bilayers are crucial for cell membrane structure and function.
    • Antibody-antigen interactions are fundamental to immune responses and diagnostics.
    • Two-dimensional crystallization is vital for high-resolution structural studies.

    Purpose of the Study:

    • To develop a method for inducing two-dimensional crystal growth of antibodies.
    • To utilize supported phospholipid bilayers on specialized electron microscopy grids.
    • To optimize conditions for antibody binding and array formation.

    Main Methods:

    • Supported phospholipid bilayers were formed on UV-irradiated, carbon-shadowed nitrocellulose grids.
    • A sequential dipping procedure transferred phospholipid monolayers from an air/water interface.

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  • Surface coverage was quantified using antibody binding assays and protein array formation.

    • Main Results:

    • UV irradiation created uniformly hydrophilic grids, facilitating bilayer formation.
    • Nearly 100% surface coverage of supported bilayers was achieved.
    • The supported bilayers demonstrated stability suitable for slow binding and long incubations.

    Conclusions:

    • Supported phospholipid bilayers on modified electron microscopy grids enable controlled antibody crystallization.
    • This technique provides a robust platform for studying antibody-antigen interactions.
    • The method is effective for achieving high-density protein arrays for binding studies.