{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T13:56:18Z","timestamp":1792504578680,"version":"4.5.0"},"reference-count":37,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2006,5,19]],"date-time":"2006-05-19T00:00:00Z","timestamp":1147996800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2006,6]]},"abstract":"<jats:p>The amyloid \u03b2 peptide (A\u03b2) is crucial for the pathogenesis of Alzheimer's disease. Aggregation of monomeric A\u03b2 into insoluble amyloid fibrils proceeds through several soluble A\u03b2 intermediates, including protofibrils, which are believed to be central in the disease process. The main reason for this is their implication in familial Alzheimer's disease with the Arctic amyloid precursor protein mutation (E693G). This mutation gives rise to early onset Alzheimer's disease, and synthetic A\u03b21\u201340Arctic displays an enhanced rate of protofibril formation <jats:italic>in vitro<\/jats:italic>[Nilsberth C, Westlind\u2010Danielsson A, Eckman CB, Condron MM, Axelman K, Forsell C, Stenh C, Luthman J, Teplow DB, Younkin SG, Naslund J &amp; Lannfelt L. (2001) <jats:italic>Nat Neurosci<\/jats:italic><jats:bold>4<\/jats:bold>, 887\u2013893]. To increase our understanding of the mechanisms involved in A\u03b2 aggregation, especially A\u03b2 monomer oligomerization into protofibrils and protofibril fibrillization into fibrils, the kinetics of A\u03b21\u201342wt and A\u03b21\u201342Arctic aggregation were examined under different physiochemical conditions, such as concentration, temperature, ionic strength and pH. We used size exclusion chromatography for this purpose, where monomers are separated from protofibrils, and fibrils are separated from protofibrils in a centrifugation step. The Arctic mutation significantly accelerated both A\u03b21\u201342wt protofibril formation and protofibril fibrillization. In addition, we demonstrated that two distinct chemical processes \u2013 monomer oligomerization and protofibril fibrillization \u2013 were affected differently by changes in the micro\u2010environment and that the Arctic mutation alters the peptide response to such changes.<\/jats:p>","DOI":"10.1111\/j.1742-4658.2006.05263.x","type":"journal-article","created":{"date-parts":[[2006,5,19]],"date-time":"2006-05-19T08:05:12Z","timestamp":1148025912000},"page":"2618-2630","source":"Crossref","is-referenced-by-count":85,"title":["Physiochemical characterization of the Alzheimer's disease\u2010related peptides A\u03b21\u201342Arctic and A\u03b21\u201342wt"],"prefix":"10.1111","volume":"273","author":[{"given":"Ann\u2010Sofi","family":"Johansson","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fredrik","family":"Berglind\u2010Dehlin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"G\u00f6ran","family":"Karlsson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katarina","family":"Edwards","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P\u00e4r","family":"Gellerfors","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lars","family":"Lannfelt","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2006,5,19]]},"reference":[{"key":"e_1_2_7_2_2","first-page":"S10","article-title":"Incidence of dementia and major subtypes in Europe: a collaborative study of population\u2010based cohorts. 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