Cargando…

Catalytically Cleavable Detergent for Membrane Protein Studies

[Image: see text] Throughout the in vitro studies of membrane proteins (MPs), proper detergents are essential for the preparation of stable aqueous samples. To date, universally applicable detergents have not yet been reported to accommodate the distinct requirements for the highly diversified MPs a...

Descripción completa

Detalles Bibliográficos
Autores principales: Liu, Lu, Zhu, Zhihao, Zhou, Fang, Xue, Dongxiang, Hu, Tao, Luo, Weiling, Qiu, Yanli, Wu, Dong, Zhao, Fei, Le, Zhiping, Tao, Houchao
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2021
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8375090/
https://www.ncbi.nlm.nih.gov/pubmed/34423216
http://dx.doi.org/10.1021/acsomega.1c02894
_version_ 1783740250146734080
author Liu, Lu
Zhu, Zhihao
Zhou, Fang
Xue, Dongxiang
Hu, Tao
Luo, Weiling
Qiu, Yanli
Wu, Dong
Zhao, Fei
Le, Zhiping
Tao, Houchao
author_facet Liu, Lu
Zhu, Zhihao
Zhou, Fang
Xue, Dongxiang
Hu, Tao
Luo, Weiling
Qiu, Yanli
Wu, Dong
Zhao, Fei
Le, Zhiping
Tao, Houchao
author_sort Liu, Lu
collection PubMed
description [Image: see text] Throughout the in vitro studies of membrane proteins (MPs), proper detergents are essential for the preparation of stable aqueous samples. To date, universally applicable detergents have not yet been reported to accommodate the distinct requirements for the highly diversified MPs and at the different stages of MP manipulation. Detergent exchange often has to be performed. We report herein the catalytically cleavable detergents (CatCDs) that can be efficiently removed to facilitate a complete exchange. To this end, functional groups, like propargyl and allyl, are introduced as branched chains or built in the hydrophobic chain close to the hydrophilic head. The representative CatCDs can be used as usual detergents in the extraction and purification of MPs and later be removed upon the addition of catalytic palladium. Mediated by CatCD-1, reconstitution of a transporter protein MsbA into a series of detergents was achieved. The extension of these designs could facilitate the future optimization of other biophysics studies.
format Online
Article
Text
id pubmed-8375090
institution National Center for Biotechnology Information
language English
publishDate 2021
publisher American Chemical Society
record_format MEDLINE/PubMed
spelling pubmed-83750902021-08-20 Catalytically Cleavable Detergent for Membrane Protein Studies Liu, Lu Zhu, Zhihao Zhou, Fang Xue, Dongxiang Hu, Tao Luo, Weiling Qiu, Yanli Wu, Dong Zhao, Fei Le, Zhiping Tao, Houchao ACS Omega [Image: see text] Throughout the in vitro studies of membrane proteins (MPs), proper detergents are essential for the preparation of stable aqueous samples. To date, universally applicable detergents have not yet been reported to accommodate the distinct requirements for the highly diversified MPs and at the different stages of MP manipulation. Detergent exchange often has to be performed. We report herein the catalytically cleavable detergents (CatCDs) that can be efficiently removed to facilitate a complete exchange. To this end, functional groups, like propargyl and allyl, are introduced as branched chains or built in the hydrophobic chain close to the hydrophilic head. The representative CatCDs can be used as usual detergents in the extraction and purification of MPs and later be removed upon the addition of catalytic palladium. Mediated by CatCD-1, reconstitution of a transporter protein MsbA into a series of detergents was achieved. The extension of these designs could facilitate the future optimization of other biophysics studies. American Chemical Society 2021-08-04 /pmc/articles/PMC8375090/ /pubmed/34423216 http://dx.doi.org/10.1021/acsomega.1c02894 Text en © 2021 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Liu, Lu
Zhu, Zhihao
Zhou, Fang
Xue, Dongxiang
Hu, Tao
Luo, Weiling
Qiu, Yanli
Wu, Dong
Zhao, Fei
Le, Zhiping
Tao, Houchao
Catalytically Cleavable Detergent for Membrane Protein Studies
title Catalytically Cleavable Detergent for Membrane Protein Studies
title_full Catalytically Cleavable Detergent for Membrane Protein Studies
title_fullStr Catalytically Cleavable Detergent for Membrane Protein Studies
title_full_unstemmed Catalytically Cleavable Detergent for Membrane Protein Studies
title_short Catalytically Cleavable Detergent for Membrane Protein Studies
title_sort catalytically cleavable detergent for membrane protein studies
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8375090/
https://www.ncbi.nlm.nih.gov/pubmed/34423216
http://dx.doi.org/10.1021/acsomega.1c02894
work_keys_str_mv AT liulu catalyticallycleavabledetergentformembraneproteinstudies
AT zhuzhihao catalyticallycleavabledetergentformembraneproteinstudies
AT zhoufang catalyticallycleavabledetergentformembraneproteinstudies
AT xuedongxiang catalyticallycleavabledetergentformembraneproteinstudies
AT hutao catalyticallycleavabledetergentformembraneproteinstudies
AT luoweiling catalyticallycleavabledetergentformembraneproteinstudies
AT qiuyanli catalyticallycleavabledetergentformembraneproteinstudies
AT wudong catalyticallycleavabledetergentformembraneproteinstudies
AT zhaofei catalyticallycleavabledetergentformembraneproteinstudies
AT lezhiping catalyticallycleavabledetergentformembraneproteinstudies
AT taohouchao catalyticallycleavabledetergentformembraneproteinstudies