title: Full membrane spanning self-assembled monolayers as model systems for UHV-based studies of cell-penetrating peptides.
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-((4'-((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)-[1,1'-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.
authors.affiliation: Max Planck Institute for Polymer Research, Mainz 55128, Germany.
authors.forename: Johannes
authors.initials: J
authors.lastname: Franz
authors.affiliation: NESAC/BIO, University of Washington, Seattle, Washington 98195.
authors.forename: Daniel J
authors.initials: DJ
authors.lastname: Graham
authors.affiliation: Max Planck Institute for Polymer Research, Mainz 55128, Germany.
authors.forename: Lars
authors.initials: L
authors.lastname: Schmüser
authors.affiliation: School of Chemical, Biological, and Environmental Engineering, Oregon State University, Corvallis, Oregon 97331.
authors.forename: Joe E
authors.initials: JE
authors.lastname: Baio
authors.affiliation: Max Planck Institute for Polymer Research, Mainz 55128, Germany.
authors.forename: Marco
authors.initials: M
authors.lastname: Lelle
authors.affiliation: Max Planck Institute for Polymer Research, Mainz 55128, Germany.
authors.forename: Kalina
authors.initials: K
authors.lastname: Peneva
authors.affiliation: Max Planck Institute for Polymer Research, Mainz 55128, Germany.
authors.forename: Klaus
authors.initials: K
authors.lastname: Müllen
authors.affiliation: NESAC/BIO, University of Washington, Seattle, Washington 98195.
authors.forename: David G
authors.initials: DG
authors.lastname: Castner
authors.affiliation: Max Planck Institute for Polymer Research, Mainz 55128, Germany.
authors.forename: Mischa
authors.initials: M
authors.lastname: Bonn
authors.affiliation: Max Planck Institute for Polymer Research, Mainz 55128, Germany.
authors.forename: Tobias
authors.initials: T
authors.lastname: Weidner
mesh_terms: D055592:Biophysical Phenomena; D057846:Cell-Penetrating Peptides / Q000378:metabolism*; D006046:Gold / Q000737:chemistry; D013058:Mass Spectrometry; D008566:Membranes / Q000737:chemistry / Q000378:metabolism*; D056951:Photoelectron Spectroscopy; D021381:Protein Transport; D056928:X-Ray Absorption Spectroscopy
chemical_list: D057846:Cell-Penetrating Peptides; D006046:Gold