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Temperature-Dependent Structural Variability of Prion Protein Amyloid Fibrils

Life Sciences Center, Institute of Biotechnology, Vilnius University, LT-10257 Vilnius, Lithuania
Author to whom correspondence should be addressed.
Academic Editor: Vladimir N. Uversky
Int. J. Mol. Sci. 2021, 22(10), 5075;
Received: 20 April 2021 / Revised: 7 May 2021 / Accepted: 9 May 2021 / Published: 11 May 2021
(This article belongs to the Special Issue The Role of Environment in Amyloid Aggregation)
Prion protein aggregation into amyloid fibrils is associated with the onset and progression of prion diseases—a group of neurodegenerative amyloidoses. The process of such aggregate formation is still not fully understood, especially regarding their polymorphism, an event where the same type of protein forms multiple, conformationally and morphologically distinct structures. Considering that such structural variations can greatly complicate the search for potential antiamyloid compounds, either by having specific propagation properties or stability, it is important to better understand this aggregation event. We have recently reported the ability of prion protein fibrils to obtain at least two distinct conformations under identical conditions, which raised the question if this occurrence is tied to only certain environmental conditions. In this work, we examined a large sample size of prion protein aggregation reactions under a range of temperatures and analyzed the resulting fibril dye-binding, secondary structure and morphological properties. We show that all temperature conditions lead to the formation of more than one fibril type and that this variability may depend on the state of the initial prion protein molecules. View Full-Text
Keywords: amyloids; prion proteins; protein aggregation; fibril structure amyloids; prion proteins; protein aggregation; fibril structure
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MDPI and ACS Style

Ziaunys, M.; Sakalauskas, A.; Mikalauskaite, K.; Snieckute, R.; Smirnovas, V. Temperature-Dependent Structural Variability of Prion Protein Amyloid Fibrils. Int. J. Mol. Sci. 2021, 22, 5075.

AMA Style

Ziaunys M, Sakalauskas A, Mikalauskaite K, Snieckute R, Smirnovas V. Temperature-Dependent Structural Variability of Prion Protein Amyloid Fibrils. International Journal of Molecular Sciences. 2021; 22(10):5075.

Chicago/Turabian Style

Ziaunys, Mantas, Andrius Sakalauskas, Kamile Mikalauskaite, Ruta Snieckute, and Vytautas Smirnovas. 2021. "Temperature-Dependent Structural Variability of Prion Protein Amyloid Fibrils" International Journal of Molecular Sciences 22, no. 10: 5075.

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