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  • Inducible release of particulates from liposomes using the mechanosensitive channel of large conductance and l-α-lysophosphatidylcholine

    Author(s)
    Foo, Alexander
    Battle, Andrew
    Chi, Gamma
    Hankamer, Ben
    Landsberg, Michael J.
    Martinac, Boris
    Griffith University Author(s)
    Battle, Andrew
    Year published
    2015
    Metadata
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    Abstract
    The mechanosensitive channel of large conductance (MscL) from Escherichia coli is a prototype for the mechanosensitive class of ion channels and opens one of the largest known gated transmembrane pores. As such, MscL offers the structural framework for the development of liposomal nanovalves for biotechnological applications. Here we incorporated MscL into liposomes and investigated the effects of l-α-lysophosphatidylcholine (LPC) with varying acyl chain lengths or saturation on its pore gating. This was measured by the efflux of encapsulated 5,6-carboxyfluorescein (CF) from the MscL proteoliposomes. Efflux improved in the ...
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    The mechanosensitive channel of large conductance (MscL) from Escherichia coli is a prototype for the mechanosensitive class of ion channels and opens one of the largest known gated transmembrane pores. As such, MscL offers the structural framework for the development of liposomal nanovalves for biotechnological applications. Here we incorporated MscL into liposomes and investigated the effects of l-α-lysophosphatidylcholine (LPC) with varying acyl chain lengths or saturation on its pore gating. This was measured by the efflux of encapsulated 5,6-carboxyfluorescein (CF) from the MscL proteoliposomes. Efflux improved in the presence of shorter and double-bonded LPC acyl chains. It was also dependent on the detergent concentration employed during MscL purification. MscL purified in 2 mM dodecyl β-d-maltopyranoside (DDM) had a marked increase in CF efflux compared to MscL purified in 1 mM DDM when treated with LPC. The purification conditions also resulted in increased efflux from proteoliposomes containing the G22C-MscL pore mutant channel, which requires higher membrane tension for its activation compared to WT-MscL.
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    Journal Title
    European Biophysics Journal
    Volume
    44
    Issue
    7
    DOI
    https://doi.org/10.1007/s00249-015-1055-4
    Subject
    Biochemistry and Cell Biology not elsewhere classified
    Atomic, Molecular, Nuclear, Particle and Plasma Physics
    Other Physical Sciences
    Biochemistry and Cell Biology
    Publication URI
    http://hdl.handle.net/10072/125052
    Collection
    • Journal articles

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