Adsorption of a styrene maleic acid (SMA) copolymer-stabilized phospholipid nanodisc on a solid-supported planar lipid bilayer.

Adsorption Lipid exchange Neutron reflectometry Polymer-stabilized phospholipid nanodisc Supported lipid bilayer styrene maleic acid (SMA) styrene-maleic acid lipid particle (SMALP)

Journal

Journal of colloid and interface science
ISSN: 1095-7103
Titre abrégé: J Colloid Interface Sci
Pays: United States
ID NLM: 0043125

Informations de publication

Date de publication:
15 Aug 2020
Historique:
received: 14 02 2020
revised: 02 04 2020
accepted: 03 04 2020
pubmed: 25 4 2020
medline: 25 4 2020
entrez: 25 4 2020
Statut: ppublish

Résumé

Over recent years, there has been a rapid development of membrane-mimetic systems to encapsulate and stabilize planar segments of phospholipid bilayers in solution. One such system has been the use of amphipathic copolymers to solubilize lipid bilayers into nanodiscs. The attractiveness of this system, in part, stems from the capability of these polymers to solubilize membrane proteins directly from the host cell membrane. The assumption has been that the native lipid annulus remains intact, with nanodiscs providing a snapshot of the lipid environment. Recent studies have provided evidence that phospholipids can exchange from the nanodiscs with either lipids at interfaces, or with other nanodiscs in bulk solution. Here we investigate kinetics of lipid exchange between three recently studied polymer-stabilized nanodiscs and supported lipid bilayers at the silicon-water interface. We show that lipid and polymer exchange occurs in all nanodiscs tested, although the rate and extent differs between different nanodisc types. Furthermore, we observe adsorption of nanodiscs to the supported lipid bilayer for one nanodisc system which used a polymer made using reversible addition-fragmentation chain transfer polymerization. These results have important implications in applications of polymer-stabilized nanodiscs, such as in the fabrication of solid-supported films containing membrane proteins.

Identifiants

pubmed: 32330753
pii: S0021-9797(20)30452-5
doi: 10.1016/j.jcis.2020.04.013
pmc: PMC7276985
pii:
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

272-284

Informations de copyright

Copyright © 2020 The Authors. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

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Auteurs

Stephen C L Hall (SCL)

School of Biosciences, University of Birmingham, Edgbaston, B15 2TT, UK; Diamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 ODE, UK.

Luke A Clifton (LA)

ISIS Neutron and Muon Source, Rutherford Appleton Laboratory, Didcot, OX11 0QX, UK.

Cecilia Tognoloni (C)

Department of Chemistry, University of Bath, Claverton Down, Bath, BA2 7AY, UK.

Kerrie A Morrison (KA)

Department of Chemistry, University of Bath, Claverton Down, Bath, BA2 7AY, UK.

Timothy J Knowles (TJ)

School of Biosciences, University of Birmingham, Edgbaston, B15 2TT, UK.

Christian J Kinane (CJ)

ISIS Neutron and Muon Source, Rutherford Appleton Laboratory, Didcot, OX11 0QX, UK.

Tim R Dafforn (TR)

School of Biosciences, University of Birmingham, Edgbaston, B15 2TT, UK.

Karen J Edler (KJ)

Department of Chemistry, University of Bath, Claverton Down, Bath, BA2 7AY, UK.

Thomas Arnold (T)

Diamond Light Source, Harwell Science and Innovation Campus, Didcot, OX11 ODE, UK; ISIS Neutron and Muon Source, Rutherford Appleton Laboratory, Didcot, OX11 0QX, UK; Department of Chemistry, University of Bath, Claverton Down, Bath, BA2 7AY, UK; European Spallation Source ERIC, P.O Box 176, SE-221 00 Lund, Sweden. Electronic address: thomas.arnold@ess.eu.

Classifications MeSH