Peptide-induced formation of a tethered lipid bilayer membrane on mesoporous silica
Journal article, 2015

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(ethylen e glycol))-2000 (DSPE-PEG(2000)-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 alpha-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.

Mesoporous

Vesicle fusion

Tethered lipid bilayer membrane

AH peptide

Author

Maria Wallin

Chalmers, Chemistry and Chemical Engineering, Applied Chemistry, Applied Surface Chemistry

J. H. Choi

Nanyang Technological University

S. O. Kim

Nanyang Technological University

N. J. Cho

Nanyang Technological University

Martin Andersson

Chalmers, Chemistry and Chemical Engineering, Applied Chemistry, Applied Surface Chemistry

European Biophysics Journal

0175-7571 (ISSN) 1432-1017 (eISSN)

Vol. 44 1-2 27-36

Subject Categories

Biophysics

DOI

10.1007/s00249-014-0998-1

More information

Created

10/7/2017