Fast Protein Footprinting by X‑ray Mediated Radical Trifluoromethylation

Synchrotron radiolysis generates hydroxyl radicals (•OH) that are successful footprinting reagents. Here, we describe a new reagent for the synchrotron platform, the trifluoromethyl radical (•CF3). The radical is produced by •OH displacement of •CF3 from sodium triflinate (Langlois reagent). Upon X-...

Full description

Saved in:
Bibliographic Details
Published in:Journal of the American Society for Mass Spectrometry 2020-05, Vol.31 (5), p.1019-1024
Main Authors: Cheng, Ming, Asuru, Awuri, Kiselar, Janna, Mathai, George, Chance, Mark R, Gross, Michael L
Format: Article
Language:English
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Synchrotron radiolysis generates hydroxyl radicals (•OH) that are successful footprinting reagents. Here, we describe a new reagent for the synchrotron platform, the trifluoromethyl radical (•CF3). The radical is produced by •OH displacement of •CF3 from sodium triflinate (Langlois reagent). Upon X-ray beam exposure, the reagent labels proteins extensively without any additional chemicals on a millisecond or shorter time scale. The •CF3 is comparably reactive to •OH and produces footprinting information that complements that of •OH alone. This reagent in combination with •OH should enable novel chemistry for protein footprinting on the synchrotron platform.
ISSN:1044-0305
1879-1123
DOI:10.1021/jasms.0c00085