ArticleThe journal of physical chemistry. A2025
IR Action Spectroscopy of Mass- and Mobility-Selected α-Synuclein Segments: Structure Identification in Early-Stage Oligomers via the Amide A Region.
Article in The journal of physical chemistry. A, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Action Spectroscopy of Mass-Selected Ions-From Principles to Applications.Journal of mass spectrometry : JMS · 2026Review
- Hyphenated Mass Spectrometry-Based Strategies for Characterizing Oligomers of α‑Synuclein in Parkinson's Disease.ACS central science · 2026Article
- Article
- How to Use Quantum Chemistry for Analyzing Mass Spectrometry Data.Mass spectrometry (Tokyo, Japan) · 2026Review
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4 authors.
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Abstract
Parkinson's disease (PD) is associated with protein misfolding and aggregation of α-Synuclein (α-Syn), a process central to its pathology. Understanding the early structural transitions of α-Syn is crucial, yet detailed insights into oligomeric intermediates remain elusive. Using the novel Photo-Synapt spectrometer, which integrates ion mobility mass spectrometry (IM-MS) with infrared multiple-photon dissociation (IRMPD) spectroscopy, we investigated the secondary structures of key α-Syn peptide segments, namely, WT-PD1 (NACore) and WT-PD2 (pre-NAC). This unique approach enabled conformationally selective analysis, allowing peptide monomers and oligomers to be separated based on both mass and mobility. Despite sequence similarities, these peptides exhibit distinct monomeric structures and aggregation behavior, leading to different oligomer assemblies with unique IR signatures. By analyzing the amide A region (3100-3500 cm
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