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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


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

Dominique-Maurice Kehlenbeck
  • The Hamburg Centre for Ultrafast Imaging and Department of Chemistry, Institute for Biochemistry and Molecular Biology, University of Hamburg, Martin-Luther-King-Platz 6, 20146 Hamburg, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Inokentijs Josts
  • The Hamburg Centre for Ultrafast Imaging and Department of Chemistry, Institute for Biochemistry and Molecular Biology, University of Hamburg, Martin-Luther-King-Platz 6, 20146 Hamburg, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Julius Nitsche
  • The Hamburg Centre for Ultrafast Imaging and Department of Chemistry, Institute for Biochemistry and Molecular Biology, University of Hamburg, Martin-Luther-King-Platz 6, 20146 Hamburg, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Sebastian Busch
  • German Engineering Materials Science Centre (GEMS) at Heinz Maier-Leibnitz Zentrum (MLZ), Helmholtz-Zentrum Geesthacht, Lichtenbergstr. 1, 85747 Garching bei München, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ V. Trevor Forsyth
  • Life Sciences Group, Institut Laue-Langevin, 6 Rue Jules Horowitz, 38042 Grenoble, France
  • School of Life Sciences, Keele University, Staffordshire ST5 5BG, England
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Henning TidowORCID iD: https://orcid.org/0000-0002-4702-9332
Published Online: 2019-06-19 | DOI: https://doi.org/10.1515/hsz-2019-0171

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.

Keywords: integral membrane proteins; MsbA; nanodiscs; Salipro; saposin-lipoprotein particles

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About the article

aInokentijs Josts and Julius Nitsche: These authors contributed equally to this work.


Received: 2019-02-26

Accepted: 2019-05-15

Published Online: 2019-06-19


Conflict of interest statement: The authors declare no competing financial interests.


Citation Information: Biological Chemistry, 20190171, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/hsz-2019-0171.

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