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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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Full membrane spanning self-assembled monolayers as model systems for UHV-based studies of cell-penetrating peptides. / Franz, Johannes; Graham, Daniel J.; Schmüser, Lars et al.

In: Biointerphases, Vol. 10, No. 1, 019009, 03.2015.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Vancouver

Franz J, Graham DJ, Schmüser L, Baio JE, Lelle M, Peneva K et al. Full membrane spanning self-assembled monolayers as model systems for UHV-based studies of cell-penetrating peptides. Biointerphases. 2015 Mar;10(1):019009. doi: 10.1116/1.4908164

Author

Franz, Johannes ; Graham, Daniel J. ; Schmüser, Lars et al. / Full membrane spanning self-assembled monolayers as model systems for UHV-based studies of cell-penetrating peptides. In: Biointerphases. 2015 ; Vol. 10, No. 1.

Bibtex

@article{53b739dcbec6421080a9633a73cd7cba,

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-((40-((5-methyl-1-phenyl-35-(phytanyl) oxy6,9,12,15,18,21,24,27,30,33,37- undecaoxa-2,3-dithiahenpentacontan-51-yl) oxy)-[1,10-biphenyl]-4yl) 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. (C) 2015 American Vacuum Society.",

keywords = "SUM-FREQUENCY GENERATION, TERMINATED ORGANIC-SURFACE, ION MASS-SPECTROMETRY, SPECTROSCOPY, ORIENTATION, ADSORPTION, GOLD, NEXAFS",

author = "Johannes Franz and Graham, {Daniel J.} and Lars Schm{\"u}ser and Baio, {Joe E.} and Marco Lelle and Kalina Peneva and Klaus Muellen and Castner, {David G.} and Mischa Bonn and Tobias Weidner",

year = "2015",

month = mar,

doi = "10.1116/1.4908164",

language = "English",

volume = "10",

journal = "Biointerphases",

issn = "1934-8630",

publisher = "AMER INST PHYSICS",

number = "1",

}

RIS

TY - JOUR

T1 - Full membrane spanning self-assembled monolayers as model systems for UHV-based studies of cell-penetrating peptides

AU - Franz, Johannes

AU - Graham, Daniel J.

AU - Schmüser, Lars

AU - Baio, Joe E.

AU - Lelle, Marco

AU - Peneva, Kalina

AU - Muellen, Klaus

AU - Castner, David G.

AU - Bonn, Mischa

AU - Weidner, Tobias

PY - 2015/3

Y1 - 2015/3

N2 - 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) oxy6,9,12,15,18,21,24,27,30,33,37- undecaoxa-2,3-dithiahenpentacontan-51-yl) oxy)-[1,10-biphenyl]-4yl) 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. (C) 2015 American Vacuum Society.

AB - 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) oxy6,9,12,15,18,21,24,27,30,33,37- undecaoxa-2,3-dithiahenpentacontan-51-yl) oxy)-[1,10-biphenyl]-4yl) 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. (C) 2015 American Vacuum Society.

KW - SUM-FREQUENCY GENERATION

KW - TERMINATED ORGANIC-SURFACE

KW - ION MASS-SPECTROMETRY

KW - SPECTROSCOPY

KW - ORIENTATION

KW - ADSORPTION

KW - GOLD

KW - NEXAFS

U2 - 10.1116/1.4908164

DO - 10.1116/1.4908164

M3 - Journal article

C2 - 25708639

VL - 10

JO - Biointerphases

JF - Biointerphases

SN - 1934-8630

IS - 1

M1 - 019009

ER -