Amyloid proteins are the etiological factors of many untreatable diseases. While structural characterization of amyloid fibrils has progressed fast, knowledge about oligomeric intermediates has lagged behind, due to their transient and dynamic nature. Mass spectrometry methods for structural biology are rapidly developing. The most relevant applications of the last 5 years are summarized and discussed here, focusing on the specific potential of the different approaches capturing oligomeric states of amyloid proteins.

Santambrogio, C., Ponzini, E., Sobott, F., Grandori, R. (2026). Recent advances in mass spectrometry methods for the investigation of oligomeric intermediates of amyloid protein aggregation. FRONTIERS IN BIOPHYSICS, 4 [10.3389/frbis.2026.1939530].

Recent advances in mass spectrometry methods for the investigation of oligomeric intermediates of amyloid protein aggregation

Santambrogio, Carlo;Ponzini, Erika;Grandori, Rita
2026

Abstract

Amyloid proteins are the etiological factors of many untreatable diseases. While structural characterization of amyloid fibrils has progressed fast, knowledge about oligomeric intermediates has lagged behind, due to their transient and dynamic nature. Mass spectrometry methods for structural biology are rapidly developing. The most relevant applications of the last 5 years are summarized and discussed here, focusing on the specific potential of the different approaches capturing oligomeric states of amyloid proteins.
Articolo in rivista - Review Essay
amyloid aggregation, amyloid β peptide, neurodegenerative diseases, oligomer structure, protein dynamics, structural mass spectrometry, transthyretin, α-synuclein
English
3-set-2026
2026
4
1939530
open
Santambrogio, C., Ponzini, E., Sobott, F., Grandori, R. (2026). Recent advances in mass spectrometry methods for the investigation of oligomeric intermediates of amyloid protein aggregation. FRONTIERS IN BIOPHYSICS, 4 [10.3389/frbis.2026.1939530].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/627928
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