Interactions of a lytic peptide with supported lipid bilayers investigated by time-resolved evanescent wave-induced fluorescence spectroscopy

Rapson, A, Gee, M, Clayton, A and Smith, T 2016, 'Interactions of a lytic peptide with supported lipid bilayers investigated by time-resolved evanescent wave-induced fluorescence spectroscopy', Methods and Applications in Fluorescence, vol. 4, no. 4, 044001, pp. 1-20.


Document type: Journal Article
Collection: Journal Articles

Title Interactions of a lytic peptide with supported lipid bilayers investigated by time-resolved evanescent wave-induced fluorescence spectroscopy
Author(s) Rapson, A
Gee, M
Clayton, A
Smith, T
Year 2016
Journal name Methods and Applications in Fluorescence
Volume number 4
Issue number 4
Article Number 044001
Start page 1
End page 20
Total pages 20
Publisher Institute of Physics Publishing
Abstract We report investigations, using time-resolved and polarised evanescent wave-induced fluorescence methods, into the location, orientation and mobility of a fluorescently labelled form of the antimicrobial peptide, melittin, when it interacts with vesicles and supported lipid bilayers (SLBs). This melittin analogue, termed MK14-A430, was found to penetrate the lipid headgroup structure in pure, ordered-phase DPPC membranes but was located near the headgroup-water region when cholesterol was included. MK14-A430 formed lytic pores in SLBs, and an increase in pore formation with incubation time was observed through an increase in polarity and mobility of the probe. When associated with the Cholesterol-containing SLB, the probe displayed polarity and mobility that indicated a population distributed near the lipid headgroup-water interface with MK14-A430 arranged predominantly in a surface-aligned state. This study indicates that the lytic activity of MK14-A430 occurred through a pore-forming mechanism. The lipid headgroup environment experienced by the fluorescent label, where MK14-A430 displayed pore information, indicated that pore formation was best described by the toroidal pore model.
Subject Biomedical Engineering not elsewhere classified
Keyword(s) evanescent wave spectroscopy
melittin
antimicrobial peptide
DOI - identifier 10.1088/2050-6120/4/4/044001
Copyright notice © 2016 IOP Publishing Ltd
ISSN 2050-6120
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