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The self-propagation of amyloid fibrils is widely observed in the aggregation pathways of numerous amyloidogenic proteins. This propensity with plasticity in primary nucleation allows amyloid fibril polymorphism, which is correlated with the pathology\/phenotypes of patients. Because the interference with the nucleation and replication processes of amyloid fibrils can alter the amyloid structure and the outcome of the disease, these processes can be a target for developing clinical drugs. Single-molecule observations of amyloid fibril replication can be an experimental system to provide the kinetic parameters for simulation studies and confirm the effect of clinical drugs. Here, we review the single-molecule observation of the amyloid fibril replication process using fluorescence microscopy and time-lapse atomic force microscopy, including high-speed atomic force microscopy. We discussed the amyloid fibril replication process and combined single-molecule observation results with molecular dynamics simulations.<\/jats:p>","DOI":"10.1093\/jmicro\/dfac011","type":"journal-article","created":{"date-parts":[[2022,3,6]],"date-time":"2022-03-06T12:06:18Z","timestamp":1646568378000},"page":"133-141","source":"Crossref","is-referenced-by-count":5,"title":["Single-molecule observation of self-propagating amyloid fibrils"],"prefix":"10.1093","volume":"71","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9758-3975","authenticated-orcid":false,"given":"Takahiro","family":"Watanabe-Nakayama","sequence":"first","affiliation":[{"name":"Nano Life Science Institute (WPI-NanoLSI), Kanazawa University , Kakuma-machi, Kanazawa 920-1192, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8454-6155","authenticated-orcid":false,"given":"Kenjiro","family":"Ono","sequence":"additional","affiliation":[{"name":"Department of Neurology, Kanazawa University Graduate School of Medical Sciences, Kanazawa University , 13-1, Takara-machi, Kanazawa 920-8640, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2022,3,7]]},"reference":[{"key":"2022060613000464100_R1","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1038\/nature04922","article-title":"The physical basis of how prion conformations determine strain phenotypes","volume":"442","author":"Tanaka","year":"2006","journal-title":"Nature"},{"key":"2022060613000464100_R2","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1038\/nature06108","article-title":"The structural basis of yeast prion strain variants","volume":"449","author":"Toyama","year":"2007","journal-title":"Nature"},{"key":"2022060613000464100_R3","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1038\/nature20814","article-title":"Structural variation in amyloid-\u03b2 fibrils from Alzheimer\u2019s disease clinical subtypes","volume":"541","author":"Qiang","year":"2017","journal-title":"Nature"},{"key":"2022060613000464100_R4","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-019-12683-8","article-title":"Cryo-EM structure and polymorphism of A\u03b2 amyloid fibrils purified from Alzheimer\u2019s brain tissue","volume":"10","author":"Kollmer","year":"2019","journal-title":"Nat. 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