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In vitro fibrillization of Alzheimer's amyloid-beta peptide (1-42)
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Tallinn University of Technology, Estonia.
Number of Authors: 4
2015 (English)In: AIP Advances, ISSN 2158-3226, E-ISSN 2158-3226, Vol. 5, no 9, 092401Article in journal (Refereed) Published
Abstract [en]

The amyloid deposition in the form of extracellular fibrillar aggregates of amyloid-beta (A beta) peptide is a critical pathological event in Alzheimer's disease. Here, we report a systematic investigation of the effects of environmental factors on the kinetics of A beta fibrillization in vitro. The effects of A beta 42 peptide concentration, temperature, pH, added solvents and the ratio of A beta 40 and A beta 42 on the peptide fibrillization under agitated conditions was studied. The analysis show that the rate of fibril growth by monomer addition is not limited by diffusion but by rearrangement in the monomer structure, which is enhanced by low concentrations of fluorinated alcohols and characterized by the activation energy of 12 kcal/ mol. Fibrillization rate decreases at pH values below 7.0 where simultaneous protonation of His 13 and 14 inhibits fibril formation. The lag period for A beta 42 was only twofold shorter and the fibril growth rate twofold faster than those of A beta 40. Lag period was shortened and the fibrillization rate was increased only at 90% content of A beta 42.

Place, publisher, year, edition, pages
2015. Vol. 5, no 9, 092401
National Category
Nano Technology Materials Engineering Physical Sciences
URN: urn:nbn:se:su:diva-122766DOI: 10.1063/1.4921071ISI: 000362562100002OAI: diva2:869042
Available from: 2015-11-12 Created: 2015-11-10 Last updated: 2015-11-12Bibliographically approved

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Tiiman, Ann
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