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  • Protein Mobility, Filtering, and Separation in Model Cell Membranes

    Fri, Jan 12, 2007 @ 01:00 PM

    Mork Family Department of Chemical Engineering and Materials Science

    Conferences, Lectures, & Seminars


    Graduate SeminarProtein Mobility, Filtering, and Separation in Model Cell MembranesDr. Susan Daniel
    Department of Chemistry
    Texas A&M UniversityAbstract
    Investigating how biomolecules behave in cell membranes gives us insight that can be used
    to create better assays, sensors, and devices that mimic the cell surface. Applications for
    these devices include rapid combinatorial analysis of drug targets, biosensors for toxin
    detection, and proteomics research. Solid-supported lipid bilayers (SLBs) are an excellent
    platform for mimicking the surface chemistry of cells. However, there are several drawbacks
    to these platforms. First, proteins can lose their mobility in these systems, impairing their
    function. Second, there is no good way to discriminate between analytes that bind to the
    same surface ligand within these platforms. Third, separation, purification, and formation of
    arrays of membrane species is difficult, impeding the progress of rapid combinatorial
    assaying of membrane proteins.
    Results will be presented on studies conducted to understand these issues and strategies to
    overcome them. By investigating the behavior of protein-protein interactions on SLBs, we
    found that protein-packing influences the point at which diffusion is arrested in these systems.
    To improve binding specificity, we devised a system for size-selective discrimination of
    protein analytes that bind to the same ligand, by incorporating poly(ethylene glycol) (PEG)
    lipopolymers into SLBs. Using our platform, we were able to achieve discrimination of
    several orders of magnitude. Finally, we developed a technique to separate membrane
    species within an SLB: bilayer chromatography. Results will be presented that show our
    separation method is sensitive enough to differentiate isomers of dye-labeled lipids and is
    currently being extended to the separation of membrane proteins.
    Friday, January 12, 2007
    1:00 p.m.
    HED 116
    The Scientific Community is Cordially Invited to Attend.

    Location: Hedco Pertroleum and Chemical Engineering Building (HED) - 116

    Audiences: Everyone Is Invited

    Contact: Petra Pearce

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