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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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  • 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)oxy- 6,9,12,15,18,21,24,27,30,33,37-undecaoxa-2,3-dithiahenpentacontan-51-yl)oxy)-[1,10-biphenyl]-4- yl)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.
  • This is the publisher’s final pdf. The article is copyrighted by the American Vacuum Society and published by the American Institute of Physics Publishing. It can be found at: http://scitation.aip.org/content/avs/journal/bip;jsessionid=1g93rvqb7shb6.x-aip-live-03.
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  • Franz, J., Graham, D. J., Schmüser, L., Baio, J. E., Lelle, M., Peneva, K., ... & Weidner, T. (2015). Full membrane spanning self-assembled monolayers as model systems for UHV-based studies of cell-penetrating peptides. Biointerphases, 10(1), 019009. doi:10.1116/1.4908164
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  • 10
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  • J.F. and T.W. thank Hao Lu for help with the XPS thickness determination and the Deutsche Forschungsgemeinschaft (WE4478/2-1) and European Union Marie Curie Program for support of this work (CIG grant #322124). This work is part of the research program of the Max Planck Society. J.F. gratefully acknowledges support by the International Max Planck Research School. D.J.G. and D.G.C. thank grant EB-002027 from the U.S. National Institutes of Health for support of the ToF-SIMS experiments. NEXAFS spectra were collected at the National Synchrotron Light Source (NSLS), Brookhaven National Laboratory, which was supported by the U.S. Department of Energy, Division of Materials Science and Division of Chemical Sciences.
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