Citation
Franz, J.; Graham, D. J.; Schmuser, L.; Baio, J. E.; Lelle, M.; Peneva, K.; Mullen, K.; Castner, D. G.; Bonn, M.; & Weidner, T. (2015). Full membrane spanning self-assembled monolayers as model systems for UHV-based studies of cell-penetrating peptides. Biointerphases, 10(1).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.Keyword(s)
Adsorptiongoldion mass-spectrometrynexafsorientationspectroscopysum-frequency generationterminated organic-surfaceNotes
Ce8alTimes Cited:2
Cited References Count:36
Reference Type
Journal ArticleSecondary Title
BiointerphasesAuthor(s)
Franz, J.Graham, D. J.Schmuser, L.Baio, J. E.Lelle, M.Peneva, K.Mullen, K.Castner, D. G.Bonn, M.Weidner, T.Year Published
2015Date Published
1425168000Volume Number
10Issue Number
1ISSN/ISBN
1934-8630DOI
Artn 01900910.1116/1.4908164