Journal
BIOMOLECULES
Volume 11, Issue 2, Pages -Publisher
MDPI
DOI: 10.3390/biom11020198
Keywords
Alzheimer's disease; amyloid beta (A beta); spherical oligomers; aggregation mechanism; morphology
Categories
Funding
- National Research Foundation of Korea (NRF) [NRF-2020R1I1A1A01065668, NRF-2017R1D1A1B03031930]
- NRF [NRF-2018R1D1A1B07051275]
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The study found that in the initial stage of aggregation process for both Aβ40 and Aβ42, multiple particles are formed which later self-assemble to form amyloid fibrils of different shapes. Different aggregation pathways of Aβ isoforms lead to amyloid fibrils with contrasting structures.
Self-aggregation of amyloid-beta (A beta) peptides has been known to play a vital role in the onset stage of neurodegenerative diseases, indicating the necessity of understanding the aggregation process of A beta peptides. Despite previous studies on the aggregation process of A beta peptides, the aggregation pathways of A beta isoforms (i.e., A beta 40 and A beta 42) and their related structures have not been fully understood yet. Here, we study the aggregation pathways of A beta 40 and A beta 42, and the structures of A beta 40 and A beta 42 aggregates during the process, based on fluorescence and atomic force microscopy (AFM) experiments. It is shown that in the beginning of aggregation process for both A beta 40 and A beta 42, a number of particles (i.e., spherical oligomers) are formed. These particles are subsequently self-assembled together, resulting in the formation of different shapes of amyloid fibrils. Our finding suggests that the different aggregation pathways of A beta isoforms lead to the amyloid fibrils with contrasting structure.
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