Open AccessDiscovery of Potent Charge-Reducing Molecules for Native Ion Mobility Mass Spectrometry Studies
Author(s) -
Jixing Lyu,
Yang Liu,
Jacob W. McCabe,
Samantha Schrecke,
Lei Fang,
David H. Russell,
Arthur Laganowsky
Publication year - 2020
Publication title -
analytical chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.117
H-Index - 332
eISSN - 1520-6882
pISSN - 0003-2700
DOI - 10.1021/acs.analchem.0c01826
Subject(s) - chemistry , ion mobility spectrometry , mass spectrometry , molecule , adduct , ion , small molecule , membrane , combinatorial chemistry , computational chemistry , chromatography , organic chemistry , biochemistry
There is growing interest in the characterization of protein complexes and their interactions with ligands using native ion mobility mass spectrometry. A particular challenge, especially for membrane proteins, is preserving noncovalent interactions and maintaining native-like structures. Different approaches have been developed to minimize activation of protein complexes by manipulating charge on protein complexes in solution and the gas-phase. Here, we report the utility of polyamines that have exceptionally high charge-reducing potencies with some molecules requiring 5-fold less than trimethylamine oxide to elicit the same effect. The charge-reducing molecules do not adduct to membrane protein complexes and are also compatible with ion-mobility mass spectrometry, paving the way for improved methods of charge reduction.