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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. Therein, 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. Moreover, 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:
 [1];  [2];  [1];  [3];  [1];  [1];  [1];  [2];  [1];  [1]
  1. Max Planck Institute for Polymer Research, Mainz (Germany)
  2. Univ. of Washington, Seattle, WA (United States). NESAC/BIO
  3. Oregon State Univ., Corvallis, OR (United States)
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL), Upton, NY (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
1229089
Report Number(s):
BNL-111164-2015-JA
Journal ID: ISSN 1934-8630; BJIOBN
DOE Contract Number:
SC00112704
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biointerphases; Journal Volume: 10; Journal Issue: 1
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 46 INSTRUMENTATION RELATED TO NUCLEAR SCIENCE AND TECHNOLOGY

Citation Formats

Franz, Johannes, Graham, Daniel J., Schmüser, Lars, Baio, Joe E., Lelle, Marco, Peneva, Kalina, Müllen, Klaus, Castner, David G., Bonn, Mischa, and Weidner, Tobias. Full membrane spanning self-assembled monolayers as model systems for UHV-based studies of cell-penetrating peptides. United States: N. p., 2015. Web. doi:10.1116/1.4908164.
Franz, Johannes, Graham, Daniel J., Schmüser, Lars, Baio, Joe E., Lelle, Marco, Peneva, Kalina, Müllen, Klaus, Castner, David G., Bonn, Mischa, & Weidner, Tobias. Full membrane spanning self-assembled monolayers as model systems for UHV-based studies of cell-penetrating peptides. United States. doi:10.1116/1.4908164.
Franz, Johannes, Graham, Daniel J., Schmüser, Lars, Baio, Joe E., Lelle, Marco, Peneva, Kalina, Müllen, Klaus, Castner, David G., Bonn, Mischa, and Weidner, Tobias. Sun . "Full membrane spanning self-assembled monolayers as model systems for UHV-based studies of cell-penetrating peptides". United States. doi:10.1116/1.4908164.
@article{osti_1229089,
title = {Full membrane spanning self-assembled monolayers as model systems for UHV-based studies of cell-penetrating peptides},
author = {Franz, Johannes and Graham, Daniel J. and Schmüser, Lars and Baio, Joe E. and Lelle, Marco and Peneva, Kalina and Müllen, Klaus and Castner, David G. and Bonn, Mischa and Weidner, Tobias},
abstractNote = {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. Therein, 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. Moreover, 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.},
doi = {10.1116/1.4908164},
journal = {Biointerphases},
number = 1,
volume = 10,
place = {United States},
year = {Sun Mar 01 00:00:00 EST 2015},
month = {Sun Mar 01 00:00:00 EST 2015}
}