Open AccessCatalytically Cleavable Detergent for Membrane Protein Studies
Author(s) -
Lei Lü,
Zhihao Zhu,
Falin Zhou,
Dongxiang Xue,
Tao Hu,
Weiling Luo,
Y. L. Qiu,
Dong Wu,
Fei Zhao,
Le Zhang,
Houchao Tao
Publication year - 2021
Publication title -
acs omega
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.779
H-Index - 40
ISSN - 2470-1343
DOI - 10.1021/acsomega.1c02894
Subject(s) - chemistry , propargyl , membrane , combinatorial chemistry , extraction (chemistry) , membrane protein , aqueous solution , chromatography , biochemistry , catalysis , organic chemistry
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.