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These disorders are named after the characteristic cross\u2010\u03b2\u2010sheet amyloid fibrils that accumulate systemically or are localized to specific organs. In most cases, current treatment is limited to symptomatic approaches and thus disease\u2010modifying therapies are needed. Alzheimer's disease is a neurodegenerative disorder with extracellular amyloid \u03b2\u2010peptide (A\u03b2) fibrils and intracellular tau neurofibrillary tangles as pathological hallmarks. Numerous clinical trials have been conducted with passive and active immunotherapy, and small molecules to inhibit A\u03b2 formation and aggregation or to enhance A\u03b2 clearance; so far such clinical trials have been unsuccessful. Novel strategies are therefore required and here we will discuss the possibility of utilizing the chaperone <jats:styled-content style=\"fixed-case\">BRICHOS<\/jats:styled-content> to prevent A\u03b2 aggregation and toxicity. Type 2 diabetes mellitus is symptomatically treated with insulin. However, the underlying pathology is linked to the aggregation and progressive accumulation of islet amyloid polypeptide as fibrils and oligomers, which are cytotoxic. Several compounds have been shown to inhibit islet amyloid aggregation and cytotoxicity <jats:italic>in vitro<\/jats:italic>. Future animal studies and clinical trials have to be conducted to determine their efficacy <jats:italic>in vivo<\/jats:italic>. The transthyretin (<jats:styled-content style=\"fixed-case\">TTR<\/jats:styled-content>) amyloidoses are a group of systemic degenerative diseases compromising multiple organ systems, caused by <jats:styled-content style=\"fixed-case\">TTR<\/jats:styled-content> aggregation. Liver transplantation decreases the generation of misfolded <jats:styled-content style=\"fixed-case\">TTR<\/jats:styled-content> and improves the quality of life for a subgroup of this patient population. Compounds that stabilize the natively folded, nonamyloidogenic, tetrameric conformation of <jats:styled-content style=\"fixed-case\">TTR<\/jats:styled-content> have been developed and the drug tafamidis is available as a promising treatment.<\/jats:p>","DOI":"10.1111\/joim.12506","type":"journal-article","created":{"date-parts":[[2016,5,11]],"date-time":"2016-05-11T05:17:56Z","timestamp":1462943876000},"page":"177-202","source":"Crossref","is-referenced-by-count":84,"title":["Current and future treatment of amyloid diseases"],"prefix":"10.1111","volume":"280","author":[{"given":"M.","family":"Ankarcrona","sequence":"first","affiliation":[{"name":"Department of Neurobiology Care Sciences and Society Division of Neurogeriatrics Center for Alzheimer Research Karolinska Institutet Huddinge Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"B.","family":"Winblad","sequence":"additional","affiliation":[{"name":"Department of Neurobiology Care Sciences and Society Division of Neurogeriatrics Center for Alzheimer Research Karolinska Institutet Huddinge Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C.","family":"Monteiro","sequence":"additional","affiliation":[{"name":"Department of Chemistry The Skaggs Institute for Chemical Biology La Jolla CA USA"},{"name":"Department of Molecular and Experimental Medicine The Scripps Research Institute La Jolla CA USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C.","family":"Fearns","sequence":"additional","affiliation":[{"name":"Department of Chemistry The Skaggs Institute for Chemical Biology La Jolla CA USA"},{"name":"Department of Molecular and Experimental Medicine The Scripps Research Institute La Jolla CA USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"E. 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