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• W2324885764 abstract "The insertion of fully folded and assembled ion channels and pores into planar lipid bilayers for electrical recording has been facilitated by the use of conventional detergents at a final concentration below the critical micelle concentration (CMC). After the desired number of channels or pores (often one) has been incorporated into a bilayer, it is important to prevent further insertion events, which is often done by awkward techniques such as perfusion. Here, we show that the addition of single-chain fluorinated amphiphiles (F-amphiphiles) with zwitterionic, simple neutral, and neutral oligomeric headgroups at a concentration above the CMC prevents the further insertion of staphylococcal α-hemolysin pores, MspA pores, and Kcv potassium channels into lipid bilayers. We found the commercially available F6FC (fluorinated fos-choline with a C6F13C2H4 chain) to be the least perturbing and most effective agent for this purpose. Bilayers are known to be resistant to F-amphiphiles, which in this case we suppose sequester the pores and channels within amphiphile aggregates. We suggest that F-amphiphiles might be useful in the fabrication of bilayer arrays for nanopore sensor devices and the rapid screening of membrane proteins." @default.
• W2324885764 created "2016-06-24" @default.
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• W2324885764 date "2011-01-28" @default.
• W2324885764 modified "2023-09-27" @default.
• W2324885764 title "Fluorinated Amphiphiles Control the Insertion of α-Hemolysin Pores into Lipid Bilayers" @default.
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• W2324885764 doi "https://doi.org/10.1021/bi1012386" @default.
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