Single molecule measurements of channel proteins incorporated into biomimetic polymermembranes
Identifieur interne : 000964 ( Istex/Checkpoint ); précédent : 000963; suivant : 000965Single molecule measurements of channel proteins incorporated into biomimetic polymermembranes
Auteurs : Denise Wong [États-Unis] ; Tae-Joon Jeon [États-Unis] ; Jacob Schmidt [États-Unis]Source :
- Nanotechnology [ 0957-4484 ] ; 2006.
English descriptors
- Teeft :
- Alamethicin, Alamethicin monomers, Average conductance, Bilayer, Bilayers, Biol, Biophys, Biosensors chem, Channel conductance, Channel incorporation, Channel proteins, Channel reconstitution, Chem, Conductance, Conductance data, Conductance jumps, Conductance states, Copolymer, Dphpc, Dphpc membranes, Energy transduction, Gating, Gating voltage, Hydrophilic block, Hydrophobic, Hydrophobic portion, Hydrophobic region, Incorporation, Lipid, Lipid bilayer membrane, Lipid bilayer membranes, Lipid membrane, Lipid membranes, Lipid solution, Long polymer, Membrane, Membrane channel, Membrane composition, Membrane formation, Membrane portion, Membrane proteins, Membrane resistance, Membrane thickness, Monomeric pores, Multiple conductance levels, Natl acad, Ompg, Open state, Other alamethicin monomers, Planar, Planar lipid bilayers, Planar membranes, Polymer, Polymer environment, Polymer membrane, Polymer membranes, Polymer molecule, Polymer molecules, Polymer vesicles, Pore, Pore formation, Pore proteins, Porin, Present work, Previous studies, Previous work, Protein pores, Reconstitution, Several minutes, Short polymer, Short polymer membrane, Shorter polymer, Single channel incorporation, Staphylococcus aureus, Thicker membranes, Transmembrane, Triblock copolymer membranes langmuir, Vesicle, Voltage gating.
Abstract
Lipid bilayer membranes have been extensively utilized to examine membrane channel andpore proteins and are the subjects of study in their own right. There has been considerablerecent interest in developing technologies to substitute or strengthen lipid bilayer membranesfor a number of applications, including sensing or drug delivery. In particular, biomimeticamphiphilic block co-polymers have been shown to have the capacity to form membranestructures and to contain membrane proteins within them. In this work, we describe thecreation of biomimetic membranes from a 5.7nm thick tri-block co-polymer and theinvestigation of the effects of the polymer environment on incorporated channel proteins(-haemolysin, OmpG, and alamethicin) with single molecule transport measurements. Wefound that the polymer membranes consistently have seal resistances of tens ofG and greater, and that the conductance of single channels is reduced by approximately 10from that measured in diphytanoyl phosphatidylcholine lipid membranes, possibly as aresult of increased cohesion of the polymer compared to lipid. The voltage gating abilityand threshold voltages of voltage gated channels were also found to be very similar in thelipid and polymer environments.
Url:
DOI: 10.1088/0957-4484/17/15/016
Affiliations:
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wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Bioengineering, University of California Los Angeles, Los Angeles, CA90095</wicri:regionArea><wicri:noRegion>CA90095</wicri:noRegion></affiliation></author><author><name sortKey="Schmidt, Jacob" sort="Schmidt, Jacob" uniqKey="Schmidt J" first="Jacob" last="Schmidt">Jacob Schmidt</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Bioengineering, University of California Los Angeles, Los Angeles, CA90095</wicri:regionArea><wicri:noRegion>CA90095</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Nanotechnology</title><title level="j" type="abbrev">Nanotechnology</title><idno type="ISSN">0957-4484</idno><idno type="eISSN">1361-6528</idno><imprint><publisher>Institute of Physics Publishing</publisher><date type="published" when="2006">2006</date><biblScope unit="volume">17</biblScope><biblScope unit="issue">15</biblScope><biblScope unit="page" from="3710">3710</biblScope><biblScope unit="page" to="3717">3717</biblScope><biblScope unit="production">Printed in the UK</biblScope></imprint><idno type="ISSN">0957-4484</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0957-4484</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Alamethicin</term><term>Alamethicin monomers</term><term>Average conductance</term><term>Bilayer</term><term>Bilayers</term><term>Biol</term><term>Biophys</term><term>Biosensors chem</term><term>Channel conductance</term><term>Channel incorporation</term><term>Channel proteins</term><term>Channel reconstitution</term><term>Chem</term><term>Conductance</term><term>Conductance data</term><term>Conductance jumps</term><term>Conductance states</term><term>Copolymer</term><term>Dphpc</term><term>Dphpc membranes</term><term>Energy transduction</term><term>Gating</term><term>Gating voltage</term><term>Hydrophilic block</term><term>Hydrophobic</term><term>Hydrophobic portion</term><term>Hydrophobic region</term><term>Incorporation</term><term>Lipid</term><term>Lipid bilayer membrane</term><term>Lipid bilayer membranes</term><term>Lipid membrane</term><term>Lipid membranes</term><term>Lipid solution</term><term>Long polymer</term><term>Membrane</term><term>Membrane channel</term><term>Membrane composition</term><term>Membrane formation</term><term>Membrane portion</term><term>Membrane proteins</term><term>Membrane resistance</term><term>Membrane thickness</term><term>Monomeric pores</term><term>Multiple conductance levels</term><term>Natl acad</term><term>Ompg</term><term>Open state</term><term>Other alamethicin monomers</term><term>Planar</term><term>Planar lipid bilayers</term><term>Planar membranes</term><term>Polymer</term><term>Polymer environment</term><term>Polymer membrane</term><term>Polymer membranes</term><term>Polymer molecule</term><term>Polymer molecules</term><term>Polymer vesicles</term><term>Pore</term><term>Pore formation</term><term>Pore proteins</term><term>Porin</term><term>Present work</term><term>Previous studies</term><term>Previous work</term><term>Protein pores</term><term>Reconstitution</term><term>Several minutes</term><term>Short polymer</term><term>Short polymer membrane</term><term>Shorter polymer</term><term>Single channel incorporation</term><term>Staphylococcus aureus</term><term>Thicker membranes</term><term>Transmembrane</term><term>Triblock copolymer membranes langmuir</term><term>Vesicle</term><term>Voltage gating</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract">Lipid bilayer membranes have been extensively utilized to examine membrane channel andpore proteins and are the subjects of study in their own right. There has been considerablerecent interest in developing technologies to substitute or strengthen lipid bilayer membranesfor a number of applications, including sensing or drug delivery. In particular, biomimeticamphiphilic block co-polymers have been shown to have the capacity to form membranestructures and to contain membrane proteins within them. In this work, we describe thecreation of biomimetic membranes from a 5.7nm thick tri-block co-polymer and theinvestigation of the effects of the polymer environment on incorporated channel proteins(-haemolysin, OmpG, and alamethicin) with single molecule transport measurements. Wefound that the polymer membranes consistently have seal resistances of tens ofG and greater, and that the conductance of single channels is reduced by approximately 10from that measured in diphytanoyl phosphatidylcholine lipid membranes, possibly as aresult of increased cohesion of the polymer compared to lipid. The voltage gating abilityand threshold voltages of voltage gated channels were also found to be very similar in thelipid and polymer environments.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Wong, Denise" sort="Wong, Denise" uniqKey="Wong D" first="Denise" last="Wong">Denise Wong</name></noRegion><name sortKey="Jeon, Tae Joon" sort="Jeon, Tae Joon" uniqKey="Jeon T" first="Tae-Joon" last="Jeon">Tae-Joon Jeon</name><name sortKey="Schmidt, Jacob" sort="Schmidt, Jacob" uniqKey="Schmidt J" first="Jacob" last="Schmidt">Jacob Schmidt</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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