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

Foo, Alexander, Battle, Andrew R., Chi, Gamma, Hankamer, Ben, Landsberg, Michael J. and Martinac, Boris (2015) Inducible release of particulates from liposomes using the mechanosensitive channel of large conductance and l-α-lysophosphatidylcholine. European Biophysics Journal, 44 7: 521-530. doi:10.1007/s00249-015-1055-4


Author Foo, Alexander
Battle, Andrew R.
Chi, Gamma
Hankamer, Ben
Landsberg, Michael J.
Martinac, Boris
Title Inducible release of particulates from liposomes using the mechanosensitive channel of large conductance and l-α-lysophosphatidylcholine
Journal name European Biophysics Journal   Check publisher's open access policy
ISSN 1432-1017
0175-7571
Publication date 2015-07-05
Sub-type Article (original research)
DOI 10.1007/s00249-015-1055-4
Volume 44
Issue 7
Start page 521
End page 530
Total pages 10
Place of publication Heidelberg, Germany
Publisher Springer
Collection year 2016
Language eng
Formatted 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 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.
Keyword Efflux
Liposomes
LPC
Mechanosensation
MscL
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2016 Collection
School of Biomedical Sciences Publications
Institute for Molecular Bioscience - Publications
 
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