{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T13:28:45Z","timestamp":1790861325785,"version":"4.1.0"},"reference-count":80,"publisher":"Wiley","license":[{"start":{"date-parts":[[2024,6,22]],"date-time":"2024-06-22T00:00:00Z","timestamp":1719014400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R35 GM138162"],"award-info":[{"award-number":["R35 GM138162"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Small Science"],"abstract":"<jats:p>Aggregation of the amyloid \u03b2 (A\u03b2) peptide into fibrils represents one of the major biochemical pathways underlying the development of Alzheimer's disease (AD). Extensive studies have been carried out to understand the role of fibrillar seeds on the overall kinetics of amyloid aggregation. However, the precise effect of seeds that are structurally or sequentially different from A\u03b2 on the structure of the resulting amyloid aggregates is yet to be fully understood. Herein, nanoscale infrared spectroscopy is used to probe the spectral facets of individual aggregates formed by aggregating A\u03b242 with antiparallel fibrillar seeds of A\u03b2(16\u201322) and E22Q A\u03b2(1\u201340) Dutch mutant and it is demonstrated that A\u03b2 can form heterotypic or mixed polymorphs that deviate significantly from its expected parallel cross \u03b2 structure. It is further shown that the formation of heterotypic aggregates is not limited to the coaggregation of A\u03b2 and its isomers, and that the former can form heterotypic fibrils with alpha\u2010synuclein and brain protein lysates. These findings highlight the complexity of A\u03b2 aggregation in AD and underscore the need to explore how A\u03b2 interacts with other brain components, which is crucial for developing better therapeutic strategies for AD.<\/jats:p>","DOI":"10.1002\/smsc.202400109","type":"journal-article","created":{"date-parts":[[2024,6,22]],"date-time":"2024-06-22T05:26:11Z","timestamp":1719033971000},"source":"Crossref","is-referenced-by-count":6,"title":["Heterotypic Seeding Generates Mixed Amyloid Polymorphs"],"prefix":"10.1002","author":[{"given":"Siddhartha","family":"Banerjee","sequence":"first","affiliation":[{"name":"Department of Chemistry and Biochemistry The University of Alabama  1007E Shelby Hall Tuscaloosa AL 35487 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Divya","family":"Baghel","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry The University of Alabama  1007E Shelby Hall Tuscaloosa AL 35487 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Harrison O.","family":"Edmonds","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry The University of Alabama  1007E Shelby Hall Tuscaloosa AL 35487 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9458-3910","authenticated-orcid":false,"given":"Ayanjeet","family":"Ghosh","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biochemistry The University of Alabama  1007E Shelby Hall Tuscaloosa AL 35487 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2024,6,22]]},"reference":[{"key":"e_1_2_8_2_1","doi-asserted-by":"publisher","DOI":"10.1002\/msj.20157"},{"key":"e_1_2_8_3_1","doi-asserted-by":"publisher","DOI":"10.15252\/emmm.201606210"},{"key":"e_1_2_8_4_1","doi-asserted-by":"publisher","DOI":"10.1101\/cshperspect.a006189"},{"key":"e_1_2_8_5_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1072994"},{"key":"e_1_2_8_6_1","doi-asserted-by":"publisher","DOI":"10.1038\/s41380-021-01249-0"},{"key":"e_1_2_8_7_1","doi-asserted-by":"publisher","DOI":"10.1038\/aps.2017.28"},{"key":"e_1_2_8_8_1","doi-asserted-by":"publisher","DOI":"10.1101\/cshperspect.a024083"},{"key":"e_1_2_8_9_1","doi-asserted-by":"publisher","DOI":"10.1038\/nsmb.1799"},{"key":"e_1_2_8_10_1","doi-asserted-by":"publisher","DOI":"10.1021\/cr3000994"},{"key":"e_1_2_8_11_1","doi-asserted-by":"publisher","DOI":"10.3390\/molecules27061776"},{"key":"e_1_2_8_12_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00069a001"},{"key":"e_1_2_8_13_1","doi-asserted-by":"publisher","DOI":"10.1021\/ja109679q"},{"key":"e_1_2_8_14_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1105850"},{"key":"e_1_2_8_15_1","doi-asserted-by":"publisher","DOI":"10.1038\/nature20814"},{"key":"e_1_2_8_16_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2023089118"},{"key":"e_1_2_8_17_1","doi-asserted-by":"publisher","DOI":"10.1039\/C4SC02517B"},{"key":"e_1_2_8_18_1","doi-asserted-by":"publisher","DOI":"10.1039\/C7SC01743J"},{"key":"e_1_2_8_19_1","doi-asserted-by":"publisher","DOI":"10.1021\/jacs.7b13660"},{"key":"e_1_2_8_20_1","doi-asserted-by":"publisher","DOI":"10.1039\/C9SC05905A"},{"key":"e_1_2_8_21_1","doi-asserted-by":"publisher","DOI":"10.1186\/s40035-022-00303-3"},{"key":"e_1_2_8_22_1","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-017-10422-x"},{"key":"e_1_2_8_23_1","doi-asserted-by":"publisher","DOI":"10.1039\/D1SC02990H"},{"key":"e_1_2_8_24_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi0011330"},{"key":"e_1_2_8_25_1","doi-asserted-by":"publisher","DOI":"10.1021\/acs.jpclett.2c02998"},{"key":"e_1_2_8_26_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1111305109"},{"key":"e_1_2_8_27_1","doi-asserted-by":"crossref","first-page":"101259","DOI":"10.1016\/j.jbc.2021.101259","volume":"297","author":"Irizarry B. 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