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

http://ir.library.oregonstate.edu/concern/articles/t148fj71x

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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  • 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.
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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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