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This review highlights the potential of sulfonamides, a versatile class of compounds recognized for their diverse pharmacological properties, as modulators of protein aggregation. We provide an overview of studies examining the efficacy of sulfonamide derivatives in inhibiting the aggregation of various amyloidogenic proteins, including amyloid\u2010beta, tau, alpha\u2010synuclein, insulin, and transthyretin. In vitro assays, such as Thioflavin T fluorescence and high\u2010resolution imaging techniques, have shown that certain sulfonamides can significantly inhibit fibril formation and promote the stabilization of non\u2010aggregated protein states. The potential for sulfonamides to serve as multi\u2010target agents offers new avenues for therapeutic development. By integrating findings from current research, we support a proposal that sulfonamide\u2010based compounds could play a pivotal role in addressing the multifaceted nature of amyloid\u2010related neurodegenerative diseases, paving the way for innovative therapeutic strategies.<\/jats:p>","DOI":"10.1002\/cmdc.202500324","type":"journal-article","created":{"date-parts":[[2025,9,1]],"date-time":"2025-09-01T23:24:32Z","timestamp":1756769072000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Sulfonamide Inhibitors of Amyloid Aggregation: A Promising Path against Neurodegenerative Diseases"],"prefix":"10.1002","volume":"20","author":[{"given":"Joana","family":"Smirnovien\u0117","sequence":"first","affiliation":[{"name":"Department of Biothermodynamics and Drug Design Institute of Biotechnology Life Sciences Center Vilnius University  Saul\u0117tekio av. 7 LT\u201010257 Vilnius 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