Structural Insights from Tandem Mass Spectrometry, Ion Mobility-Mass Spectrometry, and Infrared/Ultraviolet Spectroscopy on Sphingonodin I: Lasso vs Branched-Cyclic Topoisomers
نویسندگان
چکیده
Lasso peptides form a class of ribosomally synthesized and post-translationally modified (RiPPs) characterized by mechanically interlocked topology, where the C-terminal tail peptide is threaded trapped within an N-terminal macrolactam ring. Sphingonodin I lasso that has not yet been structurally using traditional structural biology tools (e.g., NMR X-ray crystallography), its biological function elucidated. In present work, we describe signatures characteristic II sphingonodin branched-cyclic analogue combination gas-phase ion tandem mass spectrometry, MS/MS, mobility TIMS, infrared, IR, ultraviolet, UV, spectroscopies). Tandem MS/MS CID experiments on yielded species with associated bi yj fragments demonstrating presence while ECD showed significant increase in hydrogen migration loop region when compared to analogue. The high-mobility resolving power TIMS permitted separation both topoisomers, adopted more compact structure than Cryogenic room-temperature IR spectroscopy evidenced different bond network between two topologies, cryogenic UV clearly demonstrated distinct phenylalanine environment for peptide.
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ژورنال
عنوان ژورنال: Journal of the American Society for Mass Spectrometry
سال: 2021
ISSN: ['1879-1123', '1044-0305']
DOI: https://doi.org/10.1021/jasms.1c00041