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Spatial and Multiplexed Characterization of Amyloidogenic Plaques by MALDI Imaging Using iprm-PASEF

Imaging Proteomics

Abstract #269 Posted on28 March 20259 May 2025 9 May 2025 14h16

Author(s)

Larissa Meyer (Presenting Author) | Institute for Surgical Pathology, University Hospital Freiburg | Breisacherstr.115 a, 79106, Freiburg, Germany
Mujia Jenny Li | Institute for Surgical Pathology, University Hospital Freiburg | Breisacherstr.115 a, 79106, Freiburg, Germany
Nadine Meier | Institute for Surgical Pathology, University Hospital Freiburg | Breisacherstr.115a, 79106, Freiburg, Germany
Tobias Feilen | Institute for Surgical Pathology, University Hospital Freiburg | Breisacherstr.115a, 79106, Freiburg, Germany
Konrad Kurowski | Institute for Surgical Pathology, University Hospital Freiburg | Breisacherstr.115a, 79106, Freiburg, Germany
Stephan Singer | Institute for Surgical Pathology, University Hospital Tübingen | Liebermeisterstr. 8 , 72076, Tübingen , Germany
Peter Bonsert | Institute for Surgical Pathology, University Hospital Freiburg | Breisacherstr.115a, 79106, Freiburg, Germany
Martin Werner | Institute for Surgical Pathology, University Hospital Freiburg | Breisacherstr.115a, 79106, Freiburg, Germany
Melanie Föll | Institute for Surgical Pathology, University Hospital Freiburg | Breisacherstr.115a, 79106, Freiburg, Germany
Oliver Schilling | Institute for Surgical Pathology, University Hospital Freiburg | Breisacherstr.115a, 79106, Freiburg, Germany

Abstract

Amyloidosis results from amyloidogenic fibril accumulation, potentially leading to organ failure. Diagnosing its subtypes is crucial yet challenging. Imaging parallel reaction monitoring (iprm)-parallel accumulation-serial fragmentation (PASEF) with MALDI-mass spectrometry imaging (MSI) enables rapid, spatially resolved, multiplexed, and antibody-independent peptide identification while preserving tissue structure. This study demonstrates its application for in situ amyloidosis characterization. A multiplexed iprm-PASEF panel was compiled using m/z values from literature and MALDI TIMS MS1 data, targeting amyloidosis-associated proteins (vitronectin, apolipoprotein E, serum amyloid P) and subtype-specific proteins (serum amyloid A, transthyretin, immunoglobulin light chain 1/2). A tissue microarray(TMA) of formalin-fixed, paraffin-embedded (FFPE) biopsies from 18 amyloidosis patients, covering ATTR, AL, and AA subtypes, was used. Further, Congo red staining was performed. MALDI TIMS MS1 imaging identified 1390 features. The iprm-PASEF panel, consisting of ten peptides, was then applied to the TMA. Eight peptides were fragmented (MS2) and confirmed via MASCOT. iprm-PASEF revealed a more localized, heterogeneous protein distribution than congo red staining, with subtype specificity for transthyretin and serum amyloid A. This study confirms iprm-PASEF's potential for spatial, multiplexed, and antibody-independent amyloidosis characterization.

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