Light-activated control of protein channel assembly mediated by membrane mechanics

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Title: Light-activated control of protein channel assembly mediated by membrane mechanics
Authors: Miller, DM
Findlay, HE
Ces, O
Templer, RH
Booth, PJ
Item Type: Journal Article
Abstract: Photochemical processes provide versatile triggers of chemical reactions. Here, we use a photoactivated lipid switch to modulate the folding and assembly of a protein channel within a model biological membrane. In contrast to the information rich field of water-soluble protein folding, there is only a limited understanding of the assembly of proteins that are integral to biological membranes. It is however possible to exploit the foreboding hydrophobic lipid environment and control membrane protein folding via lipid bilayer mechanics. Mechanical properties such as lipid chain lateral pressure influence the insertion and folding of proteins in membranes, with different stages of folding having contrasting sensitivities to the bilayer properties. Studies to date have relied on altering bilayer properties through lipid compositional changes made at equilibrium, and thus can only be made before or after folding. We show that light-activation of photoisomerisable di-(5-[[4-(4-butylphenyl)azo]phenoxy]pentyl)phosphate (4-Azo-5P) lipids influences the folding and assembly of the pentameric bacterial mechanosensitive channel MscL. The use of a photochemical reaction enables the bilayer properties to be altered during folding, which is unprecedented. This mechanical manipulation during folding, allows for optimisation of different stages of the component insertion, folding and assembly steps within the same lipid system. The photochemical approach offers the potential to control channel assembly when generating synthetic devices that exploit the mechanosensitive protein as a nanovalve.
Issue Date: 10-Nov-2016
Date of Acceptance: 15-Sep-2016
ISSN: 1361-6528
Publisher: IOP Publishing
Journal / Book Title: Nanotechnology
Volume: 27
Issue: 49
Copyright Statement: © 2016 IOP Publishing Ltd. This is an author-created, un-copyedited version of an article accepted for publication in Nanotechnology. IOP Publishing Ltd is not responsible for any errors or omissions in this version of the manuscript or any version derived from it. The definitive publisher authenticated version is available online at
Keywords: Nanoscience & Nanotechnology
MD Multidisciplinary
Publication Status: Published
Conference Place: England
Article Number: 494004
Appears in Collections:Chemistry
Biological and Biophysical Chemistry
Faculty of Natural Sciences

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