Atomic-level differences between brain parenchymal- and cerebrovascular-seeded Aβ fibrils
Open accessAbstract
Alzheimer’s disease is characterized by neuritic plaques, the main protein components of which are β-amyloid (Aβ) peptides deposited as β-sheet-rich amyloid fibrils. Cerebral Amyloid Angiopathy (CAA) consists of cerebrovascular deposits of Aβ peptides; it usually accompanies Alzheimer’s disease, though it sometimes occurs in the absence of neuritic plaques, as AD also occurs without accompanying CAA. Although neuritic plaques and vascular deposits have similar protein compositions, one of the characteristic features of amyloids is polymorphism, i.e., the ability of a single pure peptide to adopt multiple conformations in fibrils, depending on fibrillization conditions. For this reason, we asked whether the Aβ fibrils in neuritic plaques differed structurally from those in cerebral blood vessels. To address this question, we used seeding techniques, starting with amyloid-enriched material from either brain parenchyma or cerebral blood vessels (using meninges as the source). These amyloid-enriched preparations were then added to fresh, disaggregated solutions of Aβ to make replicate fibrils, as described elsewhere. Such fibrils were then studied by solid-state NMR, fiber X-ray diffraction, and other biophysical techniques. We observed chemical shift differences between parenchymal vs. vascular-seeded replicate fibrils in select sites (in particular, Ala2, Phe4, Val12, and Gln15 side chains) in two-dimensional 13 C-13 C correlation solid-state NMR spectra, strongly indicating structural differences at these sites. X-ray diffraction studies also indicated that vascular-seeded fibrils displayed greater order than parenchyma-seeded fibrils in the “side-chain dimension” (~ 10 Å reflection), though the “hydrogen-bond dimensions” (~ 5 Å reflection) were alike. These results indicate that the different nucleation conditions at two sites in the brain, parenchyma and blood vessels, affect the fibril products that get formed at each site, possibly leading to distinct pathophysiological outcomes.
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There is no apparent correlation between the rate of amyloid removal and the incidence of ARIA-E.
“There does not appear to be a correlation between rate of amyloid removal and the incidence of ARIA-E, in contrast to what has previously been postulated 91 and as we will discuss below.”
From The amyloid hypothesis in Alzheimer disease: new insights from new therapeutics (2022) · cites this paper as [91]
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- Authors
- Scherpelz, K. P., Wang, S., Pytel, P., Madhurapantula, R. S., Srivastava, A. K., Sachleben, J. R., Orgel, J., Ishii, Y., & Meredith, S. C.
- Affiliations
- University of Chicago (US)
- University of Illinois Chicago (US)
- Illinois Institute of Technology (US)
- Tokyo Institute of Technology (JP)
- Corresponding author
- Meredith, Stephen C.
- ORCID
- Venue
- Scientific Reports
- Published
- 2021-01-08
- Volume
- 11
- Issue
- 1
- Pages
- 247-247
- ISSN
- 2045-2322 (ISSN-L)
- PMC
- PMC7794565
- OpenAlex
- W3119535153
- Cited by
- 12
- References
- 67
- Citations by year
- 2025: 1 · 2024: 2 · 2023: 1 · 2022: 6 · 2021: 2
- FWCI
- 1.73
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Scientific Reports (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Institutional Repositories DataBase (IRDB) (submittedVersion)
- Tokyo Tech Research Repository (Tokyo Institute of Technology) (submittedVersion)
- Funders
- National Institutes of Health (T32GM07281, R01AG048793)
- Alzheimer's Association (Zenith Fellowship Award)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Neurology › Intracerebral and Subarachnoid Hemorrhage Research
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- amyloid-beta fibrils, Alzheimer's disease, cerebral amyloid angiopathy, neuritic plaques, amyloid polymorphism, fibril seeding, amyloid fibril structure
- MeSH terms
- Protein Conformation, beta-Strand, Brain, Humans, Amyloid beta-Peptides, Protein Aggregates
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