Differences in α-synuclein conformational states in physiologically relevant pH/Na + concentrations and ammonium acetate solutions unveiled by native mass spectrometry

The Analyst 2026 Open access

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Authors: Erick G. Báez Bolívar, Jessica S. Fortin, Taiwo Ademola Ademoye, Scott A. McLuckey
DOI: 10.1039/d5an01336d
Cited by: 1
References: 108

Abstract

appears to play a distinctive role in the adoption of different conformational states. Early-stage oligomers (dimer, pentamer, hexamer and heptamer) were also detected. Since oligomer formation was protein-specific, wild-type α-synuclein formed dimers while truncated α-synuclein formed pentamers, hexamers and heptamers, their abundances are consistent with kinetics of aggregation reported in the literature.

Fields of Study & Subjects

Parkinson's Disease Mechanisms and Treatments Mass Spectrometry Techniques and Applications Muscle metabolism and nutrition

Publication details

Journal / source
The Analyst
Publisher
Royal Society of Chemistry (RSC)
Volume
151
Issue
6
Pages
1748–1762
Publication date
1 January 2026
Language
EN