Functional reconstitution of protein ion channels into planar polymerizable phospholipid membranes.
We demonstrate that polymerizable planar membranes permit reconstitution of protein ion channels formed by the bacterial toxins Staphylococcus aureus alpha-hemolysin (alphaHL) and Bacillus anthracis protective antigen 63. The alphaHL channel remained functional even after membrane polymerization. Surface pressure measurements suggest that the ease of forming membranes depends on membrane surface elasticity estimated from Langmuir-Blodgett monolayer pressure-area isotherms. The ability to stabilize nanoscale pores in robust ultrathin films may prove useful in single molecule sensing applications.
Shenoy
Devanand K
DK
Center for Bio/Molecular Science and Engineering, Naval Research Laboratory, 4555 Overlook Avenue SW, Washington, DC 20375, USA. dshenoy@cbmse.nrl.navy.mil
Barger
William R
WR
Singh
Alok
A
Panchal
Rekha G
RG
Misakian
Martin
M
Stanford
Vincent M
VM
Kasianowicz
John J
JJ
D000942:Antigens, Bacterial / Q000737:chemistry; D001408:Bacillus anthracis / Q000378:metabolism; D001427:Bacterial Toxins / Q000737:chemistry; D002462:Cell Membrane / Q000378:metabolism; D002463:Cell Membrane Permeability; D029968:Escherichia coli Proteins / Q000737:chemistry; D006460:Hemolysin Proteins / Q000737:chemistry; D007473:Ion Channels / Q000737:chemistry*; D007477:Ions; D008051:Lipid Bilayers; D008055:Lipids / Q000737:chemistry; D008563:Membrane Lipids / Q000737:chemistry*; D008956:Models, Chemical; D036103:Nanotechnology; D010743:Phospholipids / Q000737:chemistry*; D011108:Polymers / Q000737:chemistry*; D011312:Pressure; D013211:Staphylococcus aureus / Q000378:metabolism; D013499:Surface Properties; D013997:Time Factors
D000942:Antigens, Bacterial; D001427:Bacterial Toxins; D029968:Escherichia coli Proteins; D006460:Hemolysin Proteins; C036507:Hlya protein, E coli; D007473:Ion Channels; D007477:Ions; D008051:Lipid Bilayers; D008055:Lipids; D008563:Membrane Lipids; D010743:Phospholipids; D011108:Polymers; C030325:anthrax toxin