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Poster Presentations
Day 2, June 23（Mon.）
Room P (Maesato East, Foyer, Ocean Wing)
- 2P-PM-06
Studying Unfolding of Peptides and Glycopeptides Using Gas-Phase FRET Hyphenated with Mass Spectrometry
(ETH Zurich)
oKim Greis, Linus Busse, Lukas Benzenberg, Ri Wu, Renato Zenobi
Native mass spectrometry (MS) aims to generate biomolecular ions in the gas phase with minimal structural disturbance. This is achieved by electrospraying molecules from buffered aqueous solutions under gentle conditions. Tandem MS workflows, such as collision-induced dissociation (CID), ultraviolet photodissociation (UVPD), and electron-based activation methods (ExD), provide detailed primary structure information but struggle with three-dimensional structural analysis. Additionally, ion activation can lead to unfolding, which is rarely studied.
To investigate how collisional and photon-based activation affects peptide structure, we combined MS with Förster resonance energy transfer (FRET). This technique measures fluorescence emission of mass-to-charge selected, labeled peptides, with quenching indicating distance-dependent interactions. Time-dependent fluorescence signals reveal the extent of peptide unfolding due to activation.
Our results show that both collisions and photons cause peptide unfolding, though to a lesser extent than charge-induced unfolding. Higher-charged species are more prone to unfolding, but lower-charged species also unfold significantly when subjected to longer activation times. These findings provide guidelines for maintaining native peptide structures during MS analysis. Next, we will apply gas-phase FRET-MS to glycopeptides to explore how glycosylation affects peptide length.