Accessible Mannitol-Based Amphiphiles (MNAs) for Membrane Protein Solubilisation and Stabilisation

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

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

Harvard

Hussain, H, Du, Y, Scull, NJ, Mortensen, JS, Tarrasch, J, Bae, HE, Loland, CJ, Byrne, B, Kobilka, BK & Chae, PS 2016, 'Accessible Mannitol-Based Amphiphiles (MNAs) for Membrane Protein Solubilisation and Stabilisation', Chemistry: A European Journal, vol. 22, no. 21, pp. 7068-7073. https://doi.org/10.1002/chem.201600533

APA

Hussain, H., Du, Y., Scull, N. J., Mortensen, J. S., Tarrasch, J., Bae, H. E., Loland, C. J., Byrne, B., Kobilka, B. K., & Chae, P. S. (2016). Accessible Mannitol-Based Amphiphiles (MNAs) for Membrane Protein Solubilisation and Stabilisation. Chemistry: A European Journal, 22(21), 7068-7073. https://doi.org/10.1002/chem.201600533

Vancouver

Hussain H, Du Y, Scull NJ, Mortensen JS, Tarrasch J, Bae HE et al. Accessible Mannitol-Based Amphiphiles (MNAs) for Membrane Protein Solubilisation and Stabilisation. Chemistry: A European Journal. 2016 May 17;22(21):7068-7073. https://doi.org/10.1002/chem.201600533

Author

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. / Accessible Mannitol-Based Amphiphiles (MNAs) for Membrane Protein Solubilisation and Stabilisation. In: Chemistry: A European Journal. 2016 ; Vol. 22, No. 21. pp. 7068-7073.

Bibtex

@article{f737e691b6ba4ef49e6e16024d9b8670,
title = "Accessible Mannitol-Based Amphiphiles (MNAs) for Membrane Protein Solubilisation and Stabilisation",
abstract = "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.",
keywords = "amphiphile design, electron microscopy, membrane proteins, novel detergents, protein stabilization",
author = "Hazrat Hussain and Yang Du and Scull, {Nicola J.} and Mortensen, {Jonas S.} and Jeffrey Tarrasch and Bae, {Hyoung Eun} and Loland, {Claus J.} and Bernadette Byrne and Kobilka, {Brian K.} and Chae, {Pil Seok}",
year = "2016",
month = may,
day = "17",
doi = "10.1002/chem.201600533",
language = "English",
volume = "22",
pages = "7068--7073",
journal = "Chemistry: A European Journal",
issn = "0947-6539",
publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",
number = "21",

}

RIS

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