{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,7,31]],"date-time":"2025-07-31T00:43:40Z","timestamp":1753922620007,"version":"3.40.5"},"reference-count":41,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2021,11,1]],"date-time":"2021-11-01T00:00:00Z","timestamp":1635724800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["iubmb.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["IUBMB Life"],"published-print":{"date-parts":[[2022,8]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Alzheimer<jats:bold>'<\/jats:bold>s disease (AD) is the most prevalent and devastating neurodegenerative disease occurred in the elderly. One of the pathogenic hallmarks is senile plaques composed of amyloid\u2010\u03b2 (A\u03b2) fibrils. Single mutations resided in A\u03b2 were found in familial AD (FAD) patients that have early onset of the disease. The molecular details and properties of each FAD A\u03b2 variants are still elusive. Here, we employed collective spectroscopic techniques to examine the properties of various A\u03b240 fibrils. We generated fibrils of wild type (WT) and three FAD mutants on residue E22 including E22G, E22K, and E22Q. We monitored fibril formation by thioflavin T (ThT) assay, examined secondary structure by Fourier transform infrared and far\u2010UV circular dichroism spectroscopy, imaged fibril morphology by transmission electron microscopy, and evaluated ThT\u2010binding kinetics. In the thermal experiments, we found E22K fibrils resisted to high temperature and retained significant \u03b2\u2010sheet content than the others. E22K fibril seeds after high\u2010temperature treatment still possess the seeding property, whereas WT fibril seeds are disturbed after the treatment. Therefore, in this study we demonstrated the mutation at E22K increases the thermal stability and seeding function of amyloid fibrils.<\/jats:p>","DOI":"10.1002\/iub.2570","type":"journal-article","created":{"date-parts":[[2021,11,1]],"date-time":"2021-11-01T17:02:56Z","timestamp":1635786176000},"page":"739-747","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Amyloid\u2010\u03b240 <scp>E22K<\/scp> fibril in familial Alzheimer's disease is more thermostable and susceptible to seeding"],"prefix":"10.1002","volume":"74","author":[{"given":"Ming\u2010Che","family":"Lee","sequence":"first","affiliation":[{"name":"Genomics Research Center, Academia Sinica  Taipei Taiwan"},{"name":"Graduate Institute of Life Sciences, National Defense Medical Center  Taipei Taiwan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yi\u2010Hung","family":"Liao","sequence":"additional","affiliation":[{"name":"Genomics Research 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