Accessible Mannitol-Based Amphiphiles (MNAs) for Membrane Protein Solubilisation and Stabilisation
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Accessible Mannitol-Based Amphiphiles (MNAs) for Membrane Protein Solubilisation and Stabilisation. / Hussain, Hazrat; Du, Yang; Scull, Nicola J.; Mortensen, Jonas S.; Tarrasch, Jeffrey; Bae, Hyoung Eun; Loland, Claus J.; Byrne, Bernadette; Kobilka, Brian K.; Chae, Pil Seok.
In: Chemistry: A European Journal, Vol. 22, No. 21, 17.05.2016, p. 7068-7073.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Accessible Mannitol-Based Amphiphiles (MNAs) for Membrane Protein Solubilisation and Stabilisation
AU - Hussain, Hazrat
AU - Du, Yang
AU - Scull, Nicola J.
AU - Mortensen, Jonas S.
AU - Tarrasch, Jeffrey
AU - Bae, Hyoung Eun
AU - Loland, Claus J.
AU - Byrne, Bernadette
AU - Kobilka, Brian K.
AU - Chae, Pil Seok
PY - 2016/5/17
Y1 - 2016/5/17
N2 - Integral membrane proteins are amphipathic molecules crucial for all cellular life. The structural study of these macromolecules starts with protein extraction from the native membranes, followed by purification and crystallisation. Detergents are essential tools for these processes, but detergent-solubilised membrane proteins often denature and aggregate, resulting in loss of both structure and function. In this study, a novel class of agents, designated mannitol-based amphiphiles (MNAs), were prepared and characterised for their ability to solubilise and stabilise membrane proteins. Some of MNAs conferred enhanced stability to four membrane proteins including a G protein-coupled receptor (GPCR), the β2 adrenergic receptor (β2AR), compared to both n-dodecyl-d-maltoside (DDM) and the other MNAs. These agents were also better than DDM for electron microscopy analysis of the β2AR. The ease of preparation together with the enhanced membrane protein stabilisation efficacy demonstrates the value of these agents for future membrane protein research.
AB - Integral membrane proteins are amphipathic molecules crucial for all cellular life. The structural study of these macromolecules starts with protein extraction from the native membranes, followed by purification and crystallisation. Detergents are essential tools for these processes, but detergent-solubilised membrane proteins often denature and aggregate, resulting in loss of both structure and function. In this study, a novel class of agents, designated mannitol-based amphiphiles (MNAs), were prepared and characterised for their ability to solubilise and stabilise membrane proteins. Some of MNAs conferred enhanced stability to four membrane proteins including a G protein-coupled receptor (GPCR), the β2 adrenergic receptor (β2AR), compared to both n-dodecyl-d-maltoside (DDM) and the other MNAs. These agents were also better than DDM for electron microscopy analysis of the β2AR. The ease of preparation together with the enhanced membrane protein stabilisation efficacy demonstrates the value of these agents for future membrane protein research.
KW - amphiphile design
KW - electron microscopy
KW - membrane proteins
KW - novel detergents
KW - protein stabilization
U2 - 10.1002/chem.201600533
DO - 10.1002/chem.201600533
M3 - Journal article
C2 - 27072057
VL - 22
SP - 7068
EP - 7073
JO - Chemistry: A European Journal
JF - Chemistry: A European Journal
SN - 0947-6539
IS - 21
ER -
ID: 167922887