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Full membrane spanning self-assembled monolayers as model systems for UHV-based studies of cell-penetrating peptides

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DOI

  • Johannes Franz, Max Planck Inst Polymer Res, Max Planck Society
  • ,
  • Daniel J. Graham, Univ Washington, University of Washington, University of Washington Seattle, NESAC BIO
  • ,
  • Lars Schmüser, Max Planck Inst Polymer Res, Max Planck Society
  • ,
  • Joe E. Baio, Oregon State University
  • ,
  • Marco Lelle, Max Planck Inst Polymer Res, Max Planck Society
  • ,
  • Kalina Peneva, Max Planck Inst Polymer Res, Max Planck Society
  • ,
  • Klaus Muellen, Max Planck Inst Polymer Res, Max Planck Society
  • ,
  • David G. Castner, Univ Washington, University of Washington, University of Washington Seattle, NESAC BIO
  • ,
  • Mischa Bonn, Max Planck Inst Polymer Res, Max Planck Society
  • ,
  • Tobias Weidner

Biophysical studies of the interaction of peptides with model membranes provide a simple yet effective approach to understand the transport of peptides and peptide based drug carriers across the cell membrane. Herein, the authors discuss the use of self-assembled monolayers fabricated from the full membrane-spanning thiol (FMST) 3-((14-((40-((5-methyl-1-phenyl-35-(phytanyl) oxy6,9,12,15,18,21,24,27,30,33,37- undecaoxa-2,3-dithiahenpentacontan-51-yl) oxy)-[1,10-biphenyl]-4yl) oxy) tetradecyl) oxy)-2-(phytanyl) oxy glycerol for ultrahigh vacuum (UHV) based experiments. UHV-based methods such as electron spectroscopy and mass spectrometry can provide important information about how peptides bind and interact with membranes, especially with the hydrophobic core of a lipid bilayer. Near-edge x-ray absorption fine structure spectra and x-ray photoelectron spectroscopy (XPS) data showed that FMST forms UHV-stable and ordered films on gold. XPS and time of flight secondary ion mass spectrometry depth profiles indicated that a proline-rich amphipathic cell-penetrating peptide, known as sweet arrow peptide is located at the outer perimeter of the model membrane. (C) 2015 American Vacuum Society.

Original languageEnglish
Article number019009
JournalBiointerphases
Volume10
Issue1
Number of pages6
ISSN1934-8630
DOIs
Publication statusPublished - Mar 2015
Externally publishedYes

    Research areas

  • SUM-FREQUENCY GENERATION, TERMINATED ORGANIC-SURFACE, ION MASS-SPECTROMETRY, SPECTROSCOPY, ORIENTATION, ADSORPTION, GOLD, NEXAFS

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