ArticleJournal of the American Society for Mass Spectrometry2025
Probing the Interactions of Cytochrome c with Anionic Phospholipid Nanodiscs Using Millisecond Hydrogen-Deuterium Exchange Mass Spectrometry.
Article in Journal of the American Society for Mass Spectrometry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The interplay between the anionic phospholipid cardiolipin (CL) and cytochrome c (cyt c) holds significance in the early stages of apoptosis. Despite identification of up to four potential sites of interaction between cytochrome c and cardiolipin bearing membranes, the exact mode of interaction remains unexplained, especially given that some of the putative binding surfaces are mutually exclusive. In this study, we utilize millisecond time-resolved electrospray ionization hydrogen-deuterium exchange mass spectrometry (TRESI-HDX-MS) to investigate conformational and dynamic changes in cytochrome c in the presence of various phospholipids (DMPC, POPG, and CL) incorporated into nanodiscs. We observe that, among the proposed binding sites, the adjacent "L"- and "A"-sites exhibited a decrease in deuterium exchange, while the "N" site remained unperturbed, suggesting a specific orientation of cytochrome c with respect to cell membranes upon binding. We also demonstrate that negatively charged phospholipids with physical differences (
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