Search

Amyloidosis diseases are characterized by protein misfolding, which forms insoluble beta-sheet fibrils progressively deposited in tissues. Deposition in the form of amyloid aggregates can occur in various organs, damaging their structure and function. The hallmark of amyloidosis is aberrant interactions leading to protein aggregation and proteotoxicity. Accordingly, amyloidosis-related samples represent a valuable source of information to generate new knowledge useful for diagnostic, prognostic, and therapeutic purposes. In this scenario, we outline the path to apply computational methods and strategies based on the combination of proteomics and systems biology approaches. In addition to algorithms useful for subtyping amyloid deposits or assessing proteome recovery after drug treatment, our chapter provides workflows based on protein-protein interaction and protein co-expression network models. In particular, the main steps to reconstruct and analyze them at both functional and topological levels are described. Our chapter aims to provide tools and instructions to identify and monitor prognostic, diagnostic, and therapeutic markers and to shed light on the processes, pathways, and functions affected by amyloidogenic proteins., (© 2025. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.)