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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...

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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
Descripción
Sumario:[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.