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{Ehsan:2022:10.1002/cbic.202200027,
author = {Ehsan, M and Wang, H and Katsube, S and Munk, CF and Du, Y and Youn, T and Yoon, S and Byrne, B and Loland, CJ and Guan, L and Kobilka, BK and Chae, PS},
doi = {10.1002/cbic.202200027},
journal = {ChemBioChem: a European journal of chemical biology},
pages = {1--8},
title = {Glyco-Steroidal Amphiphiles (GSAs) for membrane protein structural study},
url = {http://dx.doi.org/10.1002/cbic.202200027},
volume = {23},
year = {2022}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Integral membrane proteins pose considerable challenges to high resolution structural analysis. Maintaining membrane proteins in their native state during protein isolation is essential for structural study of these bio-macromolecules. Detergents are the most commonly used amphiphilic compounds for stabilizing membrane proteins in solution outside a lipid bilayer. We previously introduced a glyco-diosgenin (GDN) detergent that was shown to be highly effective at stabilizing a wide range of membrane proteins. This steroidal detergent has additionally gained attention due to its compatibility with membrane protein structure study via cryo-EM. However, synthetic inconvenience limits widespread use of GDN in membrane protein study. To improve its synthetic accessibility and to further enhance detergent efficacy for protein stabilization, we designed a new class of glyco-steroid-based detergents using three steroid units: cholestanol, cholesterol and diosgenin. These new detergents were efficiently prepared and showed marked efficacy for protein stabilization in evaluation with a few model membrane proteins including two G protein-coupled receptors. Some new agents were not only superior to a gold standard detergent, DDM (n-dodecyl-β-d-maltoside), but were also more effective than the original GDN at preserving protein integrity long term. These agents represent valuable alternatives to GDN, and are likely to facilitate structural determination of challenging membrane proteins.
AU  - Ehsan,M
AU  - Wang,H
AU  - Katsube,S
AU  - Munk,CF
AU  - Du,Y
AU  - Youn,T
AU  - Yoon,S
AU  - Byrne,B
AU  - Loland,CJ
AU  - Guan,L
AU  - Kobilka,BK
AU  - Chae,PS
DO  - 10.1002/cbic.202200027
EP  - 8
PY  - 2022///
SN  - 1439-4227
SP  - 1
TI  - Glyco-Steroidal Amphiphiles (GSAs) for membrane protein structural study
T2  - ChemBioChem: a European journal of chemical biology
UR  - http://dx.doi.org/10.1002/cbic.202200027
UR  - https://www.ncbi.nlm.nih.gov/pubmed/35129249
UR  - https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cbic.202200027
UR  - http://hdl.handle.net/10044/1/95265
VL  - 23
ER  -
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