Imperial College London
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ProfessorBernadetteByrne

Faculty of Natural Sciences, Department of Life Sciences

Associate Dean (Equality, Diversity and Inclusion) for FoNS
 
 
 
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Contact

 

+44 (0)20 7594 3004b.byrne Website

 
 
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Location

 

504Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Byrne:2021:10.1371/journal.pone.0254118,
author = {Byrne, B and Cecchetti, C and Strauss, J and Stohrer, C and Naylor, C and Pryor, E and Hobbs, J and Tanley, S and Goldman, A},
doi = {10.1371/journal.pone.0254118},
journal = {PLoS One},
pages = {1--20},
title = {A novel high-throughput screen for identifying lipids that stabilise membrane proteins in detergent based solution},
url = {http://dx.doi.org/10.1371/journal.pone.0254118},
volume = {16},
year = {2021}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Membrane proteins have a range of crucial biological functions and are the target of about 60% of all prescribed drugs. For most studies, they need to be extracted out of the lipid-bilayer, e.g. by detergent solubilisation, leading to the loss of native lipids, which may disturb important protein-lipid/bilayer interactions and thus functional and structural integrity. Relipidation of membrane proteins has proven extremely successful for studying challenging targets, but the identification of suitable lipids can be expensive and laborious. Therefore, we developed a screen to aid the high-throughput identification of beneficial lipids. The screen covers a large lipid space and was designed to be suitable for a range of stability assessment methods. Here, we demonstrate its use as a tool for identifying stabilising lipids for three membrane proteins: a bacterial pyrophosphatase (Tm-PPase), a fungal purine transporter (UapA) and a human GPCR (A2AR). A2AR is stabilised by cholesteryl hemisuccinate, a lipid well known to stabilise GPCRs, validating the approach. Additionally, our screen also identified a range of new lipids which stabilised our test proteins, providing a starting point for further investigation and demonstrating its value as a novel tool for membrane protein research. The pre-dispensed screen will be made commercially available to the scientific community in future and has a number of potential applications in the field.
AU  - Byrne,B
AU  - Cecchetti,C
AU  - Strauss,J
AU  - Stohrer,C
AU  - Naylor,C
AU  - Pryor,E
AU  - Hobbs,J
AU  - Tanley,S
AU  - Goldman,A
DO  - 10.1371/journal.pone.0254118
EP  - 20
PY  - 2021///
SN  - 1932-6203
SP  - 1
TI  - A novel high-throughput screen for identifying lipids that stabilise membrane proteins in detergent based solution
T2  - PLoS One
UR  - http://dx.doi.org/10.1371/journal.pone.0254118
UR  - https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0254118
UR  - http://hdl.handle.net/10044/1/90617
VL  - 16
ER  -
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