{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,17]],"date-time":"2026-10-17T15:38:58Z","timestamp":1792251538745,"version":"4.4.0"},"reference-count":171,"publisher":"MDPI AG","issue":"12","license":[{"start":{"date-parts":[[2020,6,16]],"date-time":"2020-06-16T00:00:00Z","timestamp":1592265600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Individual Alzheimer\u2019s disease (AD) patients have been shown to have structurally distinct amyloid-\u03b2 (A\u03b2) aggregates, including fibrils, in their brain. These findings suggest the possibility of a relationship between AD progression and A\u03b2 fibril structures. Thus, the characterization of the structural dynamics of A\u03b2 could aid the development of novel therapeutic strategies and diagnosis. Protein structure and dynamics have typically been studied separately. Most of the commonly used biophysical approaches are limited in providing substantial details regarding the combination of both structure and dynamics. On the other hand, high-speed atomic force microscopy (HS-AFM), which simultaneously visualizes an individual protein structure and its dynamics in liquid in real time, can uniquely link the structure and the kinetic details, and it can also unveil novel insights. Although amyloidogenic proteins generate heterogeneously aggregated species, including transient unstable states during the aggregation process, HS-AFM elucidated the structural dynamics of individual aggregates in real time in liquid without purification and isolation. Here, we review and discuss the HS-AFM imaging of amyloid aggregation and strategies to optimize the experiments showing findings from A\u03b2 and amylin, which is associated with type II diabetes, shares some common biological features with A\u03b2, and is reported to be involved in AD.<\/jats:p>","DOI":"10.3390\/ijms21124287","type":"journal-article","created":{"date-parts":[[2020,6,16]],"date-time":"2020-06-16T13:20:43Z","timestamp":1592313643000},"page":"4287","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":53,"title":["High-Speed Atomic Force Microscopy Reveals the Structural Dynamics of the Amyloid-\u03b2 and Amylin Aggregation Pathways"],"prefix":"10.3390","volume":"21","author":[{"given":"Takahiro","family":"Watanabe-Nakayama","sequence":"first","affiliation":[{"name":"WPI Nano Life Science Institute, Kanazawa University, Kakuma-machi, Kanazawa 920-1192, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3683-1178","authenticated-orcid":false,"given":"Bikash R.","family":"Sahoo","sequence":"additional","affiliation":[{"name":"Biophysics Program, Department of Chemistry, Macromolecular Science and Engineering, and Biomedical Engineering, The University of Michigan, Ann Arbor, MI 48109-1055, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1964-1900","authenticated-orcid":false,"given":"Ayyalusamy","family":"Ramamoorthy","sequence":"additional","affiliation":[{"name":"Biophysics and Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8454-6155","authenticated-orcid":false,"given":"Kenjiro","family":"Ono","sequence":"additional","affiliation":[{"name":"Division of Neurology, Department of Internal Medicine, School of Medicine, Showa University, Hatanodai, Shinagawa district, Tokyo 142-8666, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,6,16]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1257","DOI":"10.1016\/j.cell.2013.08.035","article-title":"Molecular structure of \u03b2-amyloid fibrils in alzheimer\u2019s disease brain tissue","volume":"154","author":"Lu","year":"2013","journal-title":"Cell"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"4760","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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