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朊病毒蛋白片段107 - 143聚集体加速朊病毒蛋白片段89 - 230淀粉样原纤维的自我复制

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

作者信息

Sneideris Tomas, Ziaunys Mantas, Chu Brett K-Y, Chen Rita P-Y, Smirnovas Vytautas

机构信息

Institute of Biothechnology, Life Sciences Center, Vilnius University, LT-10257 Vilnius, Lithuania.

Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan.

出版信息

Int J Mol Sci. 2020 Oct 8;21(19):7410. doi: 10.3390/ijms21197410.

DOI:10.3390/ijms21197410
PMID:33049945
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7583978/
Abstract

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.

摘要

朊病毒蛋白淀粉样聚集体与传染性神经退行性疾病有关，即所谓的传染性海绵状脑病。天然蛋白质分子通过重折叠进行淀粉样结构的自我复制是疾病传播的可能机制。淀粉样纤维的形成和自我复制会受到许多不同因素的影响，包括其他淀粉样蛋白和肽。小鼠朊病毒蛋白片段107 - 143（PrP(107 - 143)）和89 - 230（PrP(89 - 230)）可以形成淀粉样纤维。PrP(89 - 230)淀粉样纤维中的β-折叠核心仅限于约160 - 220位残基，其N端无结构。我们使用化学动力学工具、原子力显微镜和傅里叶变换红外光谱，来研究小鼠朊病毒蛋白片段107 - 143纤维对PrP(89 - 230)聚集的影响。数据表明，短的朊病毒衍生肽的淀粉样聚集体不能引发PrP(89 - 230)的聚集；然而，它们会加速PrP(89 - 230)淀粉样纤维的自我复制。我们得出结论，PrP(107 - 143)纤维可以通过几种可能的方式促进PrP(89 - 230)淀粉样纤维的自我复制，并且这个过程值得更多关注，因为它可能在淀粉样蛋白的传播中起重要作用。

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本文引用的文献

1
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Nat Struct Mol Biol. 2020 Jun;27(6):598-602. doi: 10.1038/s41594-020-0441-5. Epub 2020 Jun 8.
2
Formation of distinct prion protein amyloid fibrils under identical experimental conditions.在相同的实验条件下形成明显的朊病毒蛋白淀粉样纤维。
Sci Rep. 2020 Mar 12;10(1):4572. doi: 10.1038/s41598-020-61663-2.
3
The Properties of α-Synuclein Secondary Nuclei Are Dominated by the Solution Conditions Rather than the Seed Fibril Strain.
α-突触核蛋白次级核的性质主要由溶液条件决定，而不是由种子纤维应变决定。
ACS Chem Neurosci. 2020 Mar 18;11(6):909-918. doi: 10.1021/acschemneuro.9b00594. Epub 2020 Feb 28.
4
Concentration-dependent polymorphism of insulin amyloid fibrils.胰岛素淀粉样纤维的浓度依赖性多态性。
PeerJ. 2019 Dec 10;7:e8208. doi: 10.7717/peerj.8208. eCollection 2019.
5
The Environment Is a Key Factor in Determining the Anti-Amyloid Efficacy of EGCG.环境是决定 EGCG 抗淀粉样蛋白功效的关键因素。
Biomolecules. 2019 Dec 11;9(12):855. doi: 10.3390/biom9120855.
6
Physical determinants of the self-replication of protein fibrils.蛋白质原纤维自我复制的物理决定因素。
Nat Phys. 2016 Sep;12(9):874-880. doi: 10.1038/nphys3828. Epub 2016 Jul 18.
7
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Lab Invest. 2019 Jul;99(7):958-970. doi: 10.1038/s41374-019-0231-z. Epub 2019 Feb 13.
8
The Properties of Amyloid-β Fibrils Are Determined by their Path of Formation.淀粉样β纤维的性质取决于其形成途径。
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9
Amyloid assembly and disassembly.淀粉样蛋白的组装与解组装。
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10
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