Affiliation:
1. TU Dortmund University Department of Chemistry and Chemical Biology Otto-Hahn-Str. 6 44227 Dortmund Germany
2. Kavli Institute for Nanoscience Discovery South Parks Rd OX1 3QU Oxford UK
3. Freie Universität Berlin Institute of Chemistry and Biochemistry Takustraße 3 14195 Berlin Germany
4. Department of Drug Chemistry and Technologies Sapienza University of Rome P.le A. Moro 5 00185 Rome Italy
Abstract
AbstractMembrane protein purification by means of detergents is key to isolating membrane‐bound therapeutic targets. The role of the detergent structure in this process, however, is not well understood. Detergents are optimized empirically, leading to failed preparations, and thereby raising costs. Here we evaluate the utility of the hydrophilic‐lipophilic balance (HLB) concept, which was introduced by Griffin in 1949, for guiding the optimization of the hydrophobic tail in first‐generation, dendritic oligoglycerol detergents ([G1] OGDs). Our findings deliver qualitative HLB guidelines for rationalizing the optimization of detergents. Moreover, [G1] OGDs exhibit strongly delipidating properties, regardless of the structure of the hydrophobic tail, which delivers a methodological enabling step for investigating binding strengths of endogenous lipids and their role for membrane protein oligomerization. Our findings will facilitate the analysis of challenging drug targets in the future.
Funder
European Research Council
Berlin University Alliance
Fonds der Chemischen Industrie
Subject
General Chemistry,Catalysis,Organic Chemistry
Cited by
6 articles.
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