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Comparison of lipidic carrier systems for integral membrane proteins – MsbA as case study

Authors
  • Kehlenbeck, Dominique-Maurice1
  • Josts, Inokentijs1,
  • Nitsche, Julius1,
  • Busch, Sebastian2
  • Forsyth, V. Trevor3, 4
  • Tidow, Henning1
  • 1 University of Hamburg, Martin-Luther-King-Platz 6 , (Germany)
  • 2 German Engineering Materials Science Centre (GEMS) at Heinz Maier-Leibnitz Zentrum (MLZ), Helmholtz-Zentrum Geesthacht, Lichtenbergstr. 1 , (Germany)
  • 3 Life Sciences Group, Institut Laue-Langevin, 6 Rue Jules Horowitz , (France)
  • 4 Keele University, England , (United Kingdom)
Type
Published Article
Journal
Biological Chemistry
Publisher
Walter de Gruyter GmbH
Publication Date
Jun 19, 2019
Volume
400
Issue
11
Pages
1509–1518
Identifiers
DOI: 10.1515/hsz-2019-0171
Source
De Gruyter
Keywords
License
Yellow

Abstract

Membrane protein research suffers from the drawback that detergents, which are commonly used to solubilize integral membrane proteins (IMPs), often lead to protein instability and reduced activity. Recently, lipid nanodiscs (NDs) and saposin-lipoprotein particles (Salipro) have emerged as alternative carrier systems that keep membrane proteins in a native-like lipidic solution environment and are suitable for biophysical and structural studies. Here, we systematically compare nanodiscs and Salipros with respect to long-term stability as well as activity and stability of the incorporated membrane protein using the ABC transporter MsbA as model system. Our results show that both systems are suitable for activity measurements as well as structural studies in solution. Based on our results we suggest screening of different lipids with respect to activity and stability of the incorporated IMP before performing structural studies.

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