Cross-linking/mass spectrometry at the crossroads
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Cross-linking/mass spectrometry at the crossroads Lolita Piersimoni 1 & Andrea Sinz 1 Received: 30 March 2020 / Revised: 1 May 2020 / Accepted: 8 May 2020 # The Author(s) 2020
Abstract Cross-linking/mass spectrometry (XL-MS) has come a long way. Originally, XL-MS was used to study relatively small, purified proteins. Meanwhile, it is employed to investigate protein-protein interactions on a proteome-wide level, giving snapshots of cellular processes. Currently, XL-MS is at the intersection of a multitude of workflows and the impact this technique has in addressing specific biological questions is steadily growing. This article is intended to give a bird’s-eye view of the current status of XL-MS, the benefits of using MS-cleavable cross-linkers, and the challenges posed in the future development of this powerful technology. We also illustrate how XL-MS can deliver valuable structural insights into protein complexes when used in combination with other structural techniques, such as electron microscopy.
Keywords Chemical cross-linking . Cleavable cross-linkers . Electron microscopy . Mass spectrometry . Protein conformation . Protein-protein interactions . Structural biology Abbreviations ApoA-I Azide-A-DSBSO BS3 BuUrBu
CBDPS CID DC4
DSBU DSS DSSO EM
Apolipoprotein A-I Azide-tagged, acid-cleavable disuccinimidyl bissulfoxide Bis(sulfosuccinimidyl)suberate 4-{3-[3-(2,5-Dioxopyrrolidine-1-yloxycarbonyl) -propyl]-ureido}-butyric acid 2,5-dioxo-pyrrolidine-1-yl ester Cyanurbiotindipropionyl succinimide Collision-induced dissociation 1,4-Bis{4-[(2,5-dioxo-1-pyrrolidinyl) oxy]-4-oxobutyl}1,4-diazoniabicyclo[2.2.2]octane Disuccinimidyldibutyric urea Disuccinimidylsuberate Disuccinimidyl sulfoxide Electron microscopy
Published in the topical collection featuring Female Role Models in Analytical Chemistry. * Andrea Sinz [email protected] 1
Department of Pharmaceutical Chemistry & Bioanalytics, Institute of Pharmacy, Charles Tanford Center, Martin Luther University Halle-Wittenberg, Kurt-Mothes-Str. 3a, 06120 Halle (Saale), Germany
HDL HDX IMAC LCAT MS MS/MS NHS PAC4
PIR SuDP XL-MS
High-density lipoprotein Hydrogen/deuterium exchange Immobilized metal ion affinity chromatography Lecithin:cholesterol acyltransferase Mass spectrometry Tandem mass spectrometry N-Hydroxysuccinimide 1,1-Bis{4-[(2,5-dioxopyrrolidin-1-yl) oxy]-4-oxobutyl}-4-ethynylpiperidin1-ium Protein interaction reporter Disuccinimidylsuccinamyl aspartyl proline Cross-linking/mass spectrometry
Cross-linking/mass spectrometry: current status and future challenges Cross-linking/mass spectrometry (XL-MS) has undergone an impressive transformation during the last two decades, developing from a niche technique to a generally accepted method for protein structure analysis. Since 2015, the number of annual publications for XL-MS has been leveling at ca. 350 (Fig. 1). Continuous improvements in cross-linking reagents [1–3], MS instrumentation [4], and software tools [5], however, have laid the foundation for the recent inroads the XL-MS
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