Catalytically Cleavable Detergent for Membrane Protein Studies,ACS Omega

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Catalytically Cleavable Detergent for Membrane Protein Studies
ACS Omega ( IF 3.7 ) Pub Date : 2021-08-04 , DOI: 10.1021/acsomega.1c02894
Lu Liu ₁ , Zhihao Zhu ₁ , Fang Zhou ₂ , Dongxiang Xue ₂ , Tao Hu _{2,

3} , Weiling Luo _{2,

3} , Yanli Qiu _{2,

3} , Dong Wu ₂ , Fei Zhao ₂ , Zhiping Le ₁ , Houchao Tao ₂

Affiliation

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.

中文翻译：

用于膜蛋白研究的可催化裂解去污剂

在整个体外膜蛋白 (MP) 的研究中，适当的去污剂对于制备稳定的水样至关重要。迄今为止，尚未报告普遍适用的洗涤剂来适应高度多样化的 MP 和 MP 操作的不同阶段的不同要求。经常需要更换清洁剂。我们在此报告了可有效去除以促进完全交换的催化可裂解洗涤剂 (CatCD)。为此，将诸如炔丙基和烯丙基等官能团作为支链引入或构建在靠近亲水头的疏水链中。代表性的 CatCD 可用作 MP 提取和纯化中的常用清洁剂，然后在添加催化钯后将其去除。由CatCD-1介导，实现了将转运蛋白 MsbA 重构为一系列去污剂。这些设计的扩展可以促进其他生物物理学研究的未来优化。

更新日期：2021-08-17

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