title: Effect of agitation on the peptide fibrillization: Alzheimer's amyloid-β peptide 1-42 but not amylin and insulin fibrils can grow under quiescent conditions.
abstract: Many peptides and proteins can form fibrillar aggregates in vitro, but only a limited number of them are forming pathological amyloid structures in vivo. We studied the fibrillization of four peptides--Alzheimer's amyloid-β (Aβ) 1-40 and 1-42, 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 Aβ40 substantially decreased, whereas the fibrillization of Aβ42 peptide continued to proceed with almost the same rate as in the agitated conditions. The reason for the different sensitivity of the in vitro fibrillization of these peptides towards agitation in the fibril growth phase remains elusive.
authors.affiliation: Department of Gene Technology, Tallinn University of Technology, Akadeemia tee 15, Tallinn, 12618, Estonia. ann.tiiman@ttu.ee
authors.forename: Ann
authors.initials: A
authors.lastname: Tiiman
authors.forename: Andra
authors.initials: A
authors.lastname: Noormägi
authors.forename: Merlin
authors.initials: M
authors.lastname: Friedemann
authors.forename: Jekaterina
authors.initials: J
authors.lastname: Krishtal
authors.forename: Peep
authors.initials: P
authors.lastname: Palumaa
authors.forename: Vello
authors.initials: V
authors.lastname: Tõugu
mesh_terms: D000544:Alzheimer Disease; D000682:Amyloid / Q000737:chemistry*; D016229:Amyloid beta-Peptides / Q000737:chemistry*; D007328:Insulin / Q000737:chemistry; D058228:Islet Amyloid Polypeptide / Q000737:chemistry; D010446:Peptide Fragments / Q000737:chemistry*
chemical_list: D000682:Amyloid; D016229:Amyloid beta-Peptides; D007328:Insulin; D058228:Islet Amyloid Polypeptide; D010446:Peptide Fragments; C075222:amyloid beta-protein (1-42)