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We studied the fibrillization of four peptides \u2013 Alzheimer's amyloid\u2010<jats:italic>\u03b2<\/jats:italic> (A<jats:italic>\u03b2<\/jats:italic>) 1\u201040 and 1\u201042, amylin and insulin. In all cases, intensive mechanical agitation of the solution initiated fast fibrillization. However, when the mixing was stopped during the fibril growth phase, the fibrillization of amylin and insulin was practically stopped, and the rate for A<jats:italic>\u03b2<\/jats:italic><jats:sub>40<\/jats:sub> substantially decreased, whereas the fibrillization of A<jats:italic>\u03b2<\/jats:italic><jats:sub>42<\/jats:sub> peptide continued to proceed with almost the same rate as in the agitated conditions. The reason for the different sensitivity of the <jats:italic>in vitro<\/jats:italic> fibrillization of these peptides towards agitation in the fibril growth phase remains elusive. Copyright \u00a9 2013 European Peptide Society and John Wiley &amp; Sons, Ltd.<\/jats:p>","DOI":"10.1002\/psc.2513","type":"journal-article","created":{"date-parts":[[2013,4,23]],"date-time":"2013-04-23T08:44:49Z","timestamp":1366706689000},"page":"386-391","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":36,"title":["Effect of agitation on the peptide fibrillization: Alzheimer's amyloid\u2010<i>\u03b2<\/i> peptide 1\u201042 but not amylin and insulin fibrils can grow under quiescent conditions"],"prefix":"10.1002","volume":"19","author":[{"given":"Ann","family":"Tiiman","sequence":"first","affiliation":[{"name":"Department of Gene Technology Tallinn University of Technology  Akadeemia tee 15 Tallinn 12618 Estonia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Andra","family":"Noorm\u00e4gi","sequence":"additional","affiliation":[{"name":"Department of Gene Technology Tallinn University of Technology  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