The nanodisc

a novel tool for membrane protein studies

Jonas Borch, Thomas Hamann

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

Udgivelsesdato: Aug
OriginalsprogEngelsk
TidsskriftBiological Chemistry
Vol/bind390
Udgave nummer8
Sider (fra-til)805-814
Antal sider9
ISSN1431-6730
DOI
StatusUdgivet - 1. aug. 2009

Fingeraftryk

Membrane Proteins
Membranes
Detergents
Biological membranes
Oligomerization
Micelles
HDL Lipoproteins
Membrane Lipids
Scaffolds
Liposomes
Monolayers
Phospholipids
Proteins
Agglomeration
Lipids
Water
Research

Citer dette

Borch, Jonas ; Hamann, Thomas. / The nanodisc : a novel tool for membrane protein studies. I: Biological Chemistry. 2009 ; Bind 390, Nr. 8. s. 805-814.
@article{3abc3f808bc411debe4e000ea68e967b,
title = "The nanodisc: a novel tool for membrane protein studies",
abstract = "A major challenge in the research on membrane-anchored and integral membrane protein complexes is to obtain these in a functionally active, water-soluble, and monodisperse form. This requires the incorporation of the membrane proteins into a native-like membrane or detergent micelle that mimics the properties of the original biological membrane. However, solubilization in detergents or reconstitution in liposomes or supported monolayers sometimes suffers from loss of activity and problematic analyses due to heterogeneity and aggregation. A developing technology termed nanodiscs exploits discoidal phospholipid bilayers encircled by a stabilizing amphipatic helical membrane scaffold protein to reconstitute membranes with integral proteins. After reconstitution, the membrane nanodisc is soluble, stable, and monodisperse. In the present review, we outline the biological inspiration for nanodiscs as discoidal high-density lipoproteins, the assembly and handling of nanodiscs, and finally their diverse biochemical applications. In our view, major advantages of nanodisc technology for integral membrane proteins is homogeneity, control of oligomerization state, access to both sides of the membrane, and control of lipids in the local membrane environment of the integral protein.",
author = "Jonas Borch and Thomas Hamann",
year = "2009",
month = "8",
day = "1",
doi = "10.1515/BC.2009.091",
language = "English",
volume = "390",
pages = "805--814",
journal = "Biological Chemistry",
issn = "1431-6730",
publisher = "Walterde Gruyter GmbH",
number = "8",

}

The nanodisc : a novel tool for membrane protein studies. / Borch, Jonas; Hamann, Thomas.

I: Biological Chemistry, Bind 390, Nr. 8, 01.08.2009, s. 805-814.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - The nanodisc

T2 - a novel tool for membrane protein studies

AU - Borch, Jonas

AU - Hamann, Thomas

PY - 2009/8/1

Y1 - 2009/8/1

N2 - A major challenge in the research on membrane-anchored and integral membrane protein complexes is to obtain these in a functionally active, water-soluble, and monodisperse form. This requires the incorporation of the membrane proteins into a native-like membrane or detergent micelle that mimics the properties of the original biological membrane. However, solubilization in detergents or reconstitution in liposomes or supported monolayers sometimes suffers from loss of activity and problematic analyses due to heterogeneity and aggregation. A developing technology termed nanodiscs exploits discoidal phospholipid bilayers encircled by a stabilizing amphipatic helical membrane scaffold protein to reconstitute membranes with integral proteins. After reconstitution, the membrane nanodisc is soluble, stable, and monodisperse. In the present review, we outline the biological inspiration for nanodiscs as discoidal high-density lipoproteins, the assembly and handling of nanodiscs, and finally their diverse biochemical applications. In our view, major advantages of nanodisc technology for integral membrane proteins is homogeneity, control of oligomerization state, access to both sides of the membrane, and control of lipids in the local membrane environment of the integral protein.

AB - A major challenge in the research on membrane-anchored and integral membrane protein complexes is to obtain these in a functionally active, water-soluble, and monodisperse form. This requires the incorporation of the membrane proteins into a native-like membrane or detergent micelle that mimics the properties of the original biological membrane. However, solubilization in detergents or reconstitution in liposomes or supported monolayers sometimes suffers from loss of activity and problematic analyses due to heterogeneity and aggregation. A developing technology termed nanodiscs exploits discoidal phospholipid bilayers encircled by a stabilizing amphipatic helical membrane scaffold protein to reconstitute membranes with integral proteins. After reconstitution, the membrane nanodisc is soluble, stable, and monodisperse. In the present review, we outline the biological inspiration for nanodiscs as discoidal high-density lipoproteins, the assembly and handling of nanodiscs, and finally their diverse biochemical applications. In our view, major advantages of nanodisc technology for integral membrane proteins is homogeneity, control of oligomerization state, access to both sides of the membrane, and control of lipids in the local membrane environment of the integral protein.

U2 - 10.1515/BC.2009.091

DO - 10.1515/BC.2009.091

M3 - Journal article

VL - 390

SP - 805

EP - 814

JO - Biological Chemistry

JF - Biological Chemistry

SN - 1431-6730

IS - 8

ER -