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The question of why some amyloids are neurotoxic while others are harmless remains open. Here, we provide a brief overview of pathological and functional brain amyloids and present a comparative analysis of their amino acid sequences based on the percentage of hydrophobic and charged residues, as well as their enrichment in glutamine, asparagine, serine, and glycine. We demonstrate that pathological and functional brain amyloid proteins, along with their amyloidogenic fragments, do not differ in amino acid composition, contrary to previous assumptions. The ability of an amyloid to cause toxicity can instead be explained by the concept of \u201cavailable targets\u201d. Evidence from studies of pathological amyloids demonstrate that their toxicity is determined not only by a loss of function but also by aberrant interactions with specific targets, such as PrPC or mitochondrial membranes. Binding to these targets triggers pathological cascades that ultimately lead to cell death. In contrast, such targets are inaccessible to functional amyloids, either because of localized translation and protein sequestration within specialized cellular structures, or because their interactions with physiological partners prevent binding to dangerous targets.<\/jats:p>","DOI":"10.3390\/ijms262110459","type":"journal-article","created":{"date-parts":[[2025,10,28]],"date-time":"2025-10-28T11:47:19Z","timestamp":1761652039000},"page":"10459","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Pathological and Functional Brain Amyloids: A New Concept Explaining the Differences"],"prefix":"10.3390","volume":"26","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7362-8857","authenticated-orcid":false,"given":"Alexey P.","family":"Galkin","sequence":"first","affiliation":[{"name":"St. Petersburg Branch, Vavilov Institute of General Genetics, Russian Academy of Sciences, 199034 St. Petersburg, Russia"},{"name":"Department of Genetics and Biotechnology, Faculty of Biology, St. Petersburg State University, 199034 St. Petersburg, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vladimir A.","family":"Mitkevich","sequence":"additional","affiliation":[{"name":"Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexander A.","family":"Makarov","sequence":"additional","affiliation":[{"name":"Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anna A.","family":"Valina","sequence":"additional","affiliation":[{"name":"St. Petersburg Branch, Vavilov Institute of General Genetics, Russian Academy of Sciences, 199034 St. Petersburg, Russia"},{"name":"Department of Genetics and Biotechnology, Faculty of Biology, St. Petersburg State University, 199034 St. Petersburg, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1444-9784","authenticated-orcid":false,"given":"Evgeniy I.","family":"Sysoev","sequence":"additional","affiliation":[{"name":"St. Petersburg Branch, Vavilov Institute of General Genetics, Russian Academy of Sciences, 199034 St. Petersburg, Russia"},{"name":"Department of Genetics and Biotechnology, Faculty of Biology, St. Petersburg State University, 199034 St. Petersburg, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,10,28]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"476","DOI":"10.1016\/j.semcdb.2011.03.011","article-title":"Amyloid in Neurodegenerative Diseases: Friend or Foe?","volume":"22","author":"Wolfe","year":"2011","journal-title":"Semin. 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