Fluorinated amphiphiles control the insertion of α-hemolysin pores into lipid bilayers.
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 (of...
| Main Authors: | , , , , , |
|---|---|
| Format: | Journal article |
| Language: | English |
| Published: |
2011
|
| _version_ | 1797058772347125760 |
|---|---|
| author | Raychaudhuri, P Li, Q Mason, A Mikhailova, E Heron, A Bayley, H |
| author_facet | Raychaudhuri, P Li, Q Mason, A Mikhailova, E Heron, A Bayley, H |
| author_sort | Raychaudhuri, P |
| collection | OXFORD |
| description | 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 F(6)FC (fluorinated fos-choline with a C(6)F(13)C(2)H(4) 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. |
| first_indexed | 2024-03-06T19:55:04Z |
| format | Journal article |
| id | oxford-uuid:2548ffa6-e1c7-4f1f-8708-f6ec5d7afbb9 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T19:55:04Z |
| publishDate | 2011 |
| record_format | dspace |
| spelling | oxford-uuid:2548ffa6-e1c7-4f1f-8708-f6ec5d7afbb92022-03-26T11:54:49ZFluorinated amphiphiles control the insertion of α-hemolysin pores into lipid bilayers.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:2548ffa6-e1c7-4f1f-8708-f6ec5d7afbb9EnglishSymplectic Elements at Oxford2011Raychaudhuri, PLi, QMason, AMikhailova, EHeron, ABayley, HThe 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 F(6)FC (fluorinated fos-choline with a C(6)F(13)C(2)H(4) 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. |
| spellingShingle | Raychaudhuri, P Li, Q Mason, A Mikhailova, E Heron, A Bayley, H Fluorinated amphiphiles control the insertion of α-hemolysin pores into lipid bilayers. |
| title | Fluorinated amphiphiles control the insertion of α-hemolysin pores into lipid bilayers. |
| title_full | Fluorinated amphiphiles control the insertion of α-hemolysin pores into lipid bilayers. |
| title_fullStr | Fluorinated amphiphiles control the insertion of α-hemolysin pores into lipid bilayers. |
| title_full_unstemmed | Fluorinated amphiphiles control the insertion of α-hemolysin pores into lipid bilayers. |
| title_short | Fluorinated amphiphiles control the insertion of α-hemolysin pores into lipid bilayers. |
| title_sort | fluorinated amphiphiles control the insertion of α hemolysin pores into lipid bilayers |
| work_keys_str_mv | AT raychaudhurip fluorinatedamphiphilescontroltheinsertionofahemolysinporesintolipidbilayers AT liq fluorinatedamphiphilescontroltheinsertionofahemolysinporesintolipidbilayers AT masona fluorinatedamphiphilescontroltheinsertionofahemolysinporesintolipidbilayers AT mikhailovae fluorinatedamphiphilescontroltheinsertionofahemolysinporesintolipidbilayers AT herona fluorinatedamphiphilescontroltheinsertionofahemolysinporesintolipidbilayers AT bayleyh fluorinatedamphiphilescontroltheinsertionofahemolysinporesintolipidbilayers |