| Title |
Self-replication of prion protein fragment 89-230 amyloid fibrils accelerated by prion protein fragment 107-143 aggregates / |
| Authors |
Šneideris, Tomas ; Žiaunys, Mantas ; Chu, Brett K-Y ; Chen, Rita P-Y ; Smirnovas, Vytautas |
| DOI |
10.3390/ijms21197410 |
| Full Text |
|
| Is Part of |
International journal of molecular sciences.. Basel : MDPI. 2020, vol. 21, iss. 19, art. no. 7410, p. [1-16].. eISSN 1422-0067 |
| Keywords [eng] |
aggregation ; amyloid ; prion ; self-replication |
| Abstract [eng] |
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. |
| Published |
Basel : MDPI |
| Type |
Journal article |
| Language |
English |
| Publication date |
2020 |
| CC license |
|
