Polyamine detergents tailored for native mass spectrometry studies of membrane proteins

Yun Zhu, Bo-Ji Peng, Smriti Kumar, Lauren Stover, Jing-Yuan Chang, Jixing Lyu, Tianqi Zhang, Samantha Schrecke, Djavdat Azizov, David H. Russell, Lei Fang () and Arthur Laganowsky ()
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Yun Zhu: Texas A&M University
Bo-Ji Peng: Texas A&M University
Smriti Kumar: Texas A&M University
Lauren Stover: Texas A&M University
Jing-Yuan Chang: Texas A&M University
Jixing Lyu: Texas A&M University
Tianqi Zhang: Texas A&M University
Samantha Schrecke: Texas A&M University
Djavdat Azizov: Texas A&M University
David H. Russell: Texas A&M University
Lei Fang: Texas A&M University
Arthur Laganowsky: Texas A&M University

Nature Communications, 2023, vol. 14, issue 1, 1-9

Abstract: Abstract Native mass spectrometry (MS) is a powerful technique for interrogating membrane protein complexes and their interactions with other molecules. A key aspect of the technique is the ability to preserve native-like structures and noncovalent interactions, which can be challenging depending on the choice of detergent. Different strategies have been employed to reduce charge on protein complexes to minimize activation and preserve non-covalent interactions. Here, we report the synthesis of a class of polyamine detergents tailored for native MS studies of membrane proteins. These detergents, a series of spermine covalently attached to various alkyl tails, are exceptional charge-reducing molecules, exhibiting a ten-fold enhanced potency over spermine. Addition of polyamine detergents to proteins solubilized in maltoside detergents results in improved, charge-reduced native mass spectra and reduced dissociation of subunits. Polyamine detergents open new opportunities to investigate membrane proteins in different detergent environments that have thwarted previous native MS studies.

Date: 2023
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DOI: 10.1038/s41467-023-41429-w

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