{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,21]],"date-time":"2026-04-21T22:01:20Z","timestamp":1776808880823,"version":"3.51.2"},"reference-count":69,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2023,3,16]],"date-time":"2023-03-16T00:00:00Z","timestamp":1678924800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R35GM142869"],"award-info":[{"award-number":["R35GM142869"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2023,4]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Abrupt aggregation of misfolded proteins is the underlying molecular cause of Alzheimer disease (AD) and Parkinson disease (PD). Both AD and PD are severe pathologies that affect millions of people around the world. A small 42 amino acid long peptide, known as amyloid \u03b2 (A\u03b2), aggregates in the frontal cortex of AD patients forming oligomers and fibrils, highly toxic protein aggregates that cause progressive neuron death. Similar aggregates of \u03b1\u2010synuclein (\u03b1\u2010Syn), a small protein that facilitates neurotransmitter release, are observed in the midbrain, hypothalamus, and thalamus of people with PD. In this study, we utilized the innovative nano\u2010Infrared imaging technique to investigate the structural organization of individual A\u03b2 and \u03b1\u2010syn fibrils <jats:italic>postmortem<\/jats:italic> extracted from brains of AD and PD patients, respectively. We observed two morphologically different A\u03b2 and \u03b1\u2010Syn fibril polymorphs in each patient's brain. One had twisted topology, whereas another exhibited flat tape\u2010like morphology. We found that both polymorphs shared the same parallel \u03b2\u2010sheet\u2010dominated secondary structure. These findings suggested that both fibril polymorphs were built from structurally similar if not identical filaments that coiled forming twisted fibrils or associated side\u2010by\u2010side in the case of straight A\u03b2 and \u03b1\u2010Syn fibrils. Nano\u2010Infrared analysis of individual protein aggregates also revealed the presence of lipids in the structure of both twisted and tape\u2010like \u03b1\u2010Syn fibrils that were not observed in any of the A\u03b2 fibril polymorphs. These findings demonstrate that lipid membranes can play a critically important role in the onset and progression of PD.<\/jats:p>","DOI":"10.1002\/pro.4598","type":"journal-article","created":{"date-parts":[[2023,2,24]],"date-time":"2023-02-24T05:21:24Z","timestamp":1677216084000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["Nanoscale imaging of individual amyloid aggregates extracted from brains of Alzheimer and Parkinson patients reveals presence of lipids in \u03b1\u2010synuclein but not in amyloid \u03b2<sub>1\u201342<\/sub> fibrils"],"prefix":"10.1002","volume":"32","author":[{"given":"Kiryl","family":"Zhaliazka","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Biophysics Texas A&amp;M University  College Station Texas 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