Full Membrane Spanning SAMs As Model Systems for UHV-Based Studies of Cell-Penetrating Peptides

TitleFull Membrane Spanning SAMs As Model Systems for UHV-Based Studies of Cell-Penetrating Peptides
Publication TypeJournal Article
Year of Publication2015
AuthorsFranz J., Graham DJ, Schmüser L., Baio J.E., Lelle M., Peneva K., Müllen K., Castner D.G., Bonn M., Weidner T.
JournalBiointerphases
Volume10
Start Page019009
Pagination019009
Abstract

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.