Gramicidin Channel Kinetics under Tension

We have measured the effect of tension on dimerization kinetics of the channel-forming peptide gramicidin A. By aspirating large unilamellar vesicles into a micropipette electrode, we are able to simultaneously monitor membrane tension and electrical activity. We find that the dimer formation rate i...

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Published inBiophysical journal Vol. 74; no. 1; pp. 328 - 337
Main Authors Goulian, M., Mesquita, O.N., Fygenson, D.K., Nielsen, C., Andersen, O.S., Libchaber, A.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 1998
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Abstract We have measured the effect of tension on dimerization kinetics of the channel-forming peptide gramicidin A. By aspirating large unilamellar vesicles into a micropipette electrode, we are able to simultaneously monitor membrane tension and electrical activity. We find that the dimer formation rate increases by a factor of 5 as tension ranges from 0 to 4 dyn/cm. The dimer lifetime also increases with tension. This behavior is well described by a phenomenological model of membrane elasticity in which tension modulates the mismatch in thickness between the gramicidin dimer and membrane.
AbstractList We have measured the effect of tension on dimerization kinetics of the channel-forming peptide gramicidin A. By aspirating large unilamellar vesicles into a micropipette electrode, we are able to simultaneously monitor membrane tension and electrical activity. We find that the dimer formation rate increases by a factor of 5 as tension ranges from 0 to 4 dyn/cm. The dimer lifetime also increases with tension. This behavior is well described by a phenomenological model of membrane elasticity in which tension modulates the mismatch in thickness between the gramicidin dimer and membrane.
We have measured the effect of tension on dimerization kinetics of the channel-forming peptide gramicidin A. By aspirating large unilamellar vesicles into a micropipette electrode, we are able to simultaneously monitor membrane tension and electrical activity. We find that the dimer formation rate increases by a factor of 5 as tension ranges from 0 to 4 dyn/cm. The dimer lifetime also increases with tension. This behavior is well described by a phenomenological model of membrane elasticity in which tension modulates the mismatch in thickness between the gramicidin dimer and membrane.
Author Mesquita, O.N.
Andersen, O.S.
Nielsen, C.
Libchaber, A.
Fygenson, D.K.
Goulian, M.
AuthorAffiliation Center for Studies in Physics and Biology, Rockefeller University, New York, New York 10021, USA. goulian@menard.rockefeller.edu
AuthorAffiliation_xml – name: Center for Studies in Physics and Biology, Rockefeller University, New York, New York 10021, USA. goulian@menard.rockefeller.edu
Author_xml – sequence: 1
  givenname: M.
  surname: Goulian
  fullname: Goulian, M.
  email: goulian@menard.rockefeller.edu
  organization: Center for Studies in Physics and Biology, Rockefeller University, New York, New York 10021
– sequence: 2
  givenname: O.N.
  surname: Mesquita
  fullname: Mesquita, O.N.
  organization: Center for Studies in Physics and Biology, Rockefeller University, New York, New York 10021
– sequence: 3
  givenname: D.K.
  surname: Fygenson
  fullname: Fygenson, D.K.
  organization: Center for Studies in Physics and Biology, Rockefeller University, New York, New York 10021
– sequence: 4
  givenname: C.
  surname: Nielsen
  fullname: Nielsen, C.
  organization: Department of Physiology and Biophysics, Cornell University Medical College, New York, New York 10021 USA
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  givenname: O.S.
  surname: Andersen
  fullname: Andersen, O.S.
  organization: Department of Physiology and Biophysics, Cornell University Medical College, New York, New York 10021 USA
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  givenname: A.
  surname: Libchaber
  fullname: Libchaber, A.
  organization: Center for Studies in Physics and Biology, Rockefeller University, New York, New York 10021
BackLink https://www.ncbi.nlm.nih.gov/pubmed/9449333$$D View this record in MEDLINE/PubMed
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  article-title: Ion movement through gramicidin A channels. Single-channel measurements at very high potentials
  publication-title: Biophys. J.
  doi: 10.1016/S0006-3495(83)84414-2
  contributor:
    fullname: Andersen
– volume: 35
  start-page: 637
  year: 1981
  ident: 10.1016/S0006-3495(98)77790-2_bib23
  article-title: Thermoelasticity of large lecithin bilayer vesicles
  publication-title: Biophys. J.
  doi: 10.1016/S0006-3495(81)84817-5
  contributor:
    fullname: Kwok
SSID ssj0012501
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Snippet We have measured the effect of tension on dimerization kinetics of the channel-forming peptide gramicidin A. By aspirating large unilamellar vesicles into a...
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StartPage 328
SubjectTerms Dimerization
Electrochemistry
Gramicidin - analogs & derivatives
Gramicidin - chemistry
Ion Channels - chemistry
Ion Channels - physiology
Lipid Bilayers
Models, Biological
Models, Molecular
Patch-Clamp Techniques - instrumentation
Phosphatidylcholines - chemistry
Probability
Stress, Mechanical
Thermodynamics
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  providerName: Elsevier
Title Gramicidin Channel Kinetics under Tension
URI https://dx.doi.org/10.1016/S0006-3495(98)77790-2
https://www.ncbi.nlm.nih.gov/pubmed/9449333
https://search.proquest.com/docview/79665605
https://pubmed.ncbi.nlm.nih.gov/PMC1299385
Volume 74
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