Nanoaggregates Derived from Amyloid-beta and Alpha-synuclein Characterized by Sequential Quadruple Force Mapping
SCIE
SCOPUS
- Title
- Nanoaggregates Derived from Amyloid-beta and Alpha-synuclein Characterized by Sequential Quadruple Force Mapping
- Authors
- Shin, Eun Ji; Park, Joon Won
- Date Issued
- 2021-05
- Publisher
- AMER CHEMICAL SOC
- Abstract
- Overlapping of Alzheimer's disease and Parkinson's disease is associated with the formation of hetero-oligomers derived from amyloid-beta and alpha-synuclein. However, the structural identity of the hetero-oligomer has yet to be elucidated, particularly at high resolution. Here, with atomic force microscopy, the surface structure of hetero-oligomer was examined with four AFM tips tethering one of the selected antibodies recognizing N-terminus or C-terminus of each peptide. All aggregates were found to be hetero-oligomers, and probability of recognizing the termini is higher than that for the homo-oligomers, suggesting that the termini of the former have a greater tendency to be located at the surface or the termini have more freedom to be recognized, probably through loose packing. The methodology in this study provides us with a new approach to elucidate the structure of such aggregates at the single-molecule level, allowing the exploration of other intrinsically disordered proteins frequently found in nature.
- Keywords
- Aggregates; Atomic force microscopy; Glycoproteins; Neurodegenerative diseases; Proteins; Surface structure; Alzheimer' s disease; High resolution; Homo-oligomers; Intrinsically disordered proteins; Nanoaggregates; New approaches; Parkinson' s disease; Single molecule level; Oligomers
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/106663
- DOI
- 10.1021/acs.nanolett.1c00058
- ISSN
- 1530-6984
- Article Type
- Article
- Citation
- NANO LETTERS, vol. 21, no. 9, page. 3789 - 3797, 2021-05
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