Imperial College London

ProfessorBernadetteByrne

Faculty of Natural SciencesDepartment of Life Sciences

Professor of Molecular Membrane Biology
 
 
 
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Contact

 

+44 (0)20 7594 3004b.byrne

 
 
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Location

 

504Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Sadaf:2019:10.1021/acschembio.9b00166,
author = {Sadaf, A and Ramos, M and Mortensen, JS and Du, Y and Bae, HE and Munk, CF and Hariharan, P and Byrne, B and Kobilka, BK and Loland, CJ and Guan, L and Chae, PS},
doi = {10.1021/acschembio.9b00166},
journal = {ACS Chemical Biology},
pages = {1717--1726},
title = {Conformationally restricted monosaccharide-cored glycoside amphiphiles: the effect of detergent headgroup variation on membrane protein stability.},
url = {http://dx.doi.org/10.1021/acschembio.9b00166},
volume = {14},
year = {2019}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Detergents are widely used to isolate membrane proteins from lipid bilayers, but many proteins solubilized in conventional detergents are structurally unstable. Thus, there is major interest in the development of novel amphiphiles to facilitate membrane protein research. In this study, we have designed and synthesized novel amphiphiles with a rigid scyllo-inositol core, designated scyllo-inositol glycosides (SIGs). Varying the headgroup structure allowed the preparation of three sets of SIGs that were evaluated for their effects on membrane protein stability. When tested with a few model membrane proteins, representative SIGs conferred enhanced stability to the membrane proteins compared to a gold standard conventional detergent (DDM). Of the novel amphiphiles, a SIG designated STM-12 was most effective at preserving the stability of the multiple membrane proteins tested here. In addition, a comparative study of the three sets suggests that several factors, including micelle size and alkyl chain length, need to be considered in the development of novel detergents for membrane protein research. Thus, this study not only describes new detergent tools that are potentially useful for membrane protein structural study but also introduces plausible correlations between the chemical properties of detergents and membrane protein stabilization efficacy.
AU - Sadaf,A
AU - Ramos,M
AU - Mortensen,JS
AU - Du,Y
AU - Bae,HE
AU - Munk,CF
AU - Hariharan,P
AU - Byrne,B
AU - Kobilka,BK
AU - Loland,CJ
AU - Guan,L
AU - Chae,PS
DO - 10.1021/acschembio.9b00166
EP - 1726
PY - 2019///
SN - 1554-8929
SP - 1717
TI - Conformationally restricted monosaccharide-cored glycoside amphiphiles: the effect of detergent headgroup variation on membrane protein stability.
T2 - ACS Chemical Biology
UR - http://dx.doi.org/10.1021/acschembio.9b00166
UR - https://www.ncbi.nlm.nih.gov/pubmed/31305987
UR - https://pubs.acs.org/doi/10.1021/acschembio.9b00166
UR - http://hdl.handle.net/10044/1/72915
VL - 14
ER -