title: Different morphology of amyloid fibrils originating from agitated and non-agitated conditions.
abstract: In vitro amyloid formation has been suggested to be a common property of any polypeptide chain depending on particular environmental conditions although in vivo amyloid fibril formation can be promoted by point mutations or triplet expansions. Here, we explored the influence of agitation on fibril formation of amyloidogenic alanine segments fused to Cold Shock Protein B (CspB) of Bacillus subtilis. While without agitation fibril formation was clearly dependent on the presence of an amyloidogenic alanine segment, fibril formation was independent of the amyloidogenic segment under agitation. Agitation even led to fibrillation of native CspB lacking the amyloidogenic segment. Furthermore, agitation not only influenced the kinetics of fibril formation, but also resulted in completely different fibril morphologies. These results indicate that experimental conditions can alter the region that undergoes a conformational change during in vitro fibrillation. Moreover, the data show that deductions from in vitro assays on in vivo fibril formation mechanisms are afflicted with a certain degree of uncertainty and therefore need to be cautiously discussed.
authors.affiliation: Facultatea de Zootehnie şi Biotehnologii, Universitatea de Ştiinţe Agricole şi Medicină Veterinară, Calea Mănăştur 3-5, 400372 Cluj-Napoca, Romania. anja.buttstedt@gmail.com
authors.forename: Anja
authors.initials: A
authors.lastname: Buttstedt
authors.forename: Tanja
authors.initials: T
authors.lastname: Wostradowski
authors.forename: Christian
authors.initials: C
authors.lastname: Ihling
authors.forename: Gerd
authors.initials: G
authors.lastname: Hause
authors.forename: Andrea
authors.initials: A
authors.lastname: Sinz
authors.forename: Elisabeth
authors.initials: E
authors.lastname: Schwarz
mesh_terms: D000409:Alanine / Q000235:genetics / Q000378:metabolism*; D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism*; D001412:Bacillus subtilis / Q000378:metabolism*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D010446:Peptide Fragments / Q000235:genetics / Q000378:metabolism*; D017510:Protein Folding; D011595:Psychomotor Agitation; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism*; D013816:Thermodynamics
chemical_list: D000682:Amyloid; D001426:Bacterial Proteins; D010446:Peptide Fragments; D011993:Recombinant Fusion Proteins; C077188:cold-shock protein CspB, Bacteria; D000409:Alanine