Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/81036
Title: Peptide-induced formation of a tethered lipid bilayer membrane on mesoporous silica
Authors: Wallin, Maria
Choi, Jae‑Hyeok
Kim, Seong Oh
Cho, Nam‑Joon
Andersson, Martin
Keywords: Mesoporous
Tethered lipid bilayer membrane
AH peptide
Vesicle fusion
Issue Date: 2014
Source: Wallin, M., Choi, J.-H., Kim, S. O., Cho, N.-J., & Andersson, M. (2015). Peptide-induced formation of a tethered lipid bilayer membrane on mesoporous silica. European Biophysics Journal, 44(1), 27-36.
Series/Report no.: European Biophysics Journal
Abstract: Tethered bilayer lipid membranes (tBLMs) on solid supports have substantial advantages as models of artificial cell membranes for such biomedical applications as drug delivery and biosensing. Compared with untethered lipid membranes, tBLMs have more space between substrate and the bilayer and greater stability. The purpose of this work was to use these properties to fabricate and characterize a zwitterionic 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine lipid tBLM containing 2 mol % 1,2-distearoyl-sn-glycero-3-phosphoethanolamine-N-maleimide(poly(ethylene glycol))-2000 (DSPE-PEG2000-NHS) lipid tethers on a 3-aminopropyltrimethoxysilane-modified mesoporous silica substrate. A quartz crystal microbalance with dissipation monitoring was used to monitor the process of vesicle adsorption and tBLM self-assembly, and atomic force microscopy was performed to characterize the structural properties of the tBLM obtained. Whereas tether-containing lipid vesicles ruptured neither spontaneously nor as a result of osmotic shock, introduction of an amphipathic α-helical (AH) peptide induced vesicle rupture and subsequent tBLM formation. Taken together, our findings suggest that the AH peptide is an efficient means of rupturing vesicles of both simple and complex composition, and is, therefore, useful for formation of tBLMs on solid and mesoporous materials for applications in biotechnology.
URI: https://hdl.handle.net/10356/81036
http://hdl.handle.net/10220/40654
ISSN: 0175-7571
DOI: 10.1007/s00249-014-0998-1
Schools: School of Chemical and Biomedical Engineering 
School of Materials Science & Engineering 
Rights: © 2014 European Biophysical Societies’ Association
Fulltext Permission: none
Fulltext Availability: No Fulltext
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