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A new azobenzene-based design strategy for detergents in membrane protein research

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Urner,  Leonhard Hagen       
Institute of Chemistry and Biochemistry, Freie Universität Berlin;
Molecular Physics, Fritz Haber Institute, Max Planck Society;
Physical and Theoretical Chemistry Laboratory, University of Oxford;

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Hoffmann,  Waldemar       
Institute of Chemistry and Biochemistry, Freie Universität Berlin;
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Warnke,  Stephan
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Pagel,  Kevin       
Institute of Chemistry and Biochemistry, Freie Universität Berlin;
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Citation

Urner, L. H., Schulze, M., Maier, Y. B., Hoffmann, W., Warnke, S., Liko, I., et al. (2020). A new azobenzene-based design strategy for detergents in membrane protein research. Chemical Science, 11(13), 3538-3546. doi:10.1039/D0SC01022G.


Cite as: https://hdl.handle.net/21.11116/0000-0005-F8C1-9
Abstract
Mass spectrometry enables the in-depth structural elucidation of membrane protein complexes, which is of great interest in structural biology and drug discovery. Recent breakthroughs in this field revealed the need for design rules that allow fine-tuning the properties of detergents in solution and gas phase. Desirable features include protein charge reduction, because it helps to preserve native features of protein complexes during transfer from solution into the vacuum of a mass spectrometer. Addressing this challenge, we here present the first systematic gas-phase study of azobenzene detergents. The utility of gas-phase techniques for monitoring light-driven changes of isomer ratios and molecular properties are investigated in detail. This leads to the first azobenzene detergent that enables the native mass spectrometry analysis of membrane proteins and whose charge-reducing properties can be tuned by irradiation with light. More broadly, the presented work outlines new avenues for the high-throughput characterization of supramolecular systems and opens a new design strategy for detergents in membrane protein research.