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Open AccessArticle

Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 Aggregates

1
Institute of Biothechnology, Life Sciences Center, Vilnius University, LT-10257 Vilnius, Lithuania
2
Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan
3
Department of Chemistry, National Taiwan University, Taipei 106, Taiwan
4
Institute of Biochemical Sciences, National Taiwan University, Taipei 106, Taiwan
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Int. J. Mol. Sci. 2020, 21(19), 7410; https://doi.org/10.3390/ijms21197410
Received: 21 August 2020 / Revised: 2 October 2020 / Accepted: 3 October 2020 / Published: 8 October 2020
(This article belongs to the Special Issue Amyloid Hetero-Aggregation)
Prion protein amyloid aggregates are associated with infectious neurodegenerative diseases, known as transmissible spongiform encephalopathies. Self-replication of amyloid structures by refolding of native protein molecules is the probable mechanism of disease transmission. Amyloid fibril formation and self-replication can be affected by many different factors, including other amyloid proteins and peptides. Mouse prion protein fragments 107-143 (PrP(107-143)) and 89-230 (PrP(89-230)) can form amyloid fibrils. β-sheet core in PrP(89-230) amyloid fibrils is limited to residues ∼160–220 with unstructured N-terminus. We employed chemical kinetics tools, atomic force microscopy and Fourier-transform infrared spectroscopy, to investigate the effects of mouse prion protein fragment 107-143 fibrils on the aggregation of PrP(89-230). The data suggest that amyloid aggregates of a short prion-derived peptide are not able to seed PrP(89-230) aggregation; however, they accelerate the self-replication of PrP(89-230) amyloid fibrils. We conclude that PrP(107-143) fibrils could facilitate the self-replication of PrP(89-230) amyloid fibrils in several possible ways, and that this process deserves more attention as it may play an important role in amyloid propagation. View Full-Text
Keywords: amyloid; prion; aggregation; self-replication amyloid; prion; aggregation; self-replication
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MDPI and ACS Style

Sneideris, T.; Ziaunys, M.; Chu, B.K.-Y.; Chen, R.P.-Y.; Smirnovas, V. Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 Aggregates. Int. J. Mol. Sci. 2020, 21, 7410. https://doi.org/10.3390/ijms21197410

AMA Style

Sneideris T, Ziaunys M, Chu BK-Y, Chen RP-Y, Smirnovas V. Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 Aggregates. International Journal of Molecular Sciences. 2020; 21(19):7410. https://doi.org/10.3390/ijms21197410

Chicago/Turabian Style

Sneideris, Tomas; Ziaunys, Mantas; Chu, Brett K.-Y.; Chen, Rita P.-Y.; Smirnovas, Vytautas. 2020. "Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 Aggregates" Int. J. Mol. Sci. 21, no. 19: 7410. https://doi.org/10.3390/ijms21197410

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