Heterotypic Seeding Generates Mixed Amyloid Polymorphs
Aggregation of the amyloid β (Aβ) peptide into fibrils represents one of the major biochemical pathways underlying the development of Alzheimer's disease (AD). Extensive studies have been carried out to understand the role of fibrillar seeds on the overall kinetics of amyloid aggregation. However, the precise effect of seeds that are structurally or sequentially different from Aβ on the structure of the resulting amyloid aggregates is yet to be fully understood. Herein, nanoscale infrared spectroscopy is used to probe the spectral facets of individual aggregates formed by aggregating Aβ42 with antiparallel fibrillar seeds of Aβ(16–22) and E22Q Aβ(1–40) Dutch mutant and it is demonstrated that Aβ can form heterotypic or mixed polymorphs that deviate significantly from its expected parallel cross β structure. It is further shown that the formation of heterotypic aggregates is not limited to the coaggregation of Aβ and its isomers, and that the former can form heterotypic fibrils with alpha‐synuclein and brain protein lysates. These findings highlight the complexity of Aβ aggregation in AD and underscore the need to explore how Aβ interacts with other brain components, which is crucial for developing better therapeutic strategies for AD.
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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Heterotypic Seeding Generates Mixed Amyloid Polymorphs ; day:22 ; month:06 ; year:2024 ; extent:12
Small science ; (22.06.2024) (gesamt 12)
- Creator
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Banerjee, Siddhartha
Baghel, Divya
Edmonds, Harrison O.
Ghosh, Ayanjeet
- DOI
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10.1002/smsc.202400109
- URN
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urn:nbn:de:101:1-2406221457059.606283411692
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 11:03 AM CEST
Data provider
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Banerjee, Siddhartha
- Baghel, Divya
- Edmonds, Harrison O.
- Ghosh, Ayanjeet
Other Objects (12)
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Loss of TREM2 function increases amyloid seeding but reduces plaque-associated ApoE
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Manual and automatic assignment of two different Aβ40 amyloid fibril polymorphs using MAS solid-state NMR spectroscopy
Maturation-dependent changes in the size, structure and seeding capacity of Aβ42 amyloid fibrils
Amyloid pathology arrangements in Alzheimer’s disease brains modulate in vivo seeding capability
Mechanism of Cellular Formation and In Vivo Seeding Effects of Hexameric β-Amyloid Assemblies
Cryo-EM analysis of the effect of seeding with brain-derived Aβ amyloid fibrils
Hierarchical Protofilament Intertwining Rules the Formation of Mixed‐Curvature Amyloid Polymorphs
Hsp70-mediated disaggregation of α-synuclein amyloid polymorphs
Dissecting aggregation and seeding dynamics of α-Syn polymorphs using the phasor approach to FLIM
Amplification of Brain Aggregated-Amyloid Beta by developing an Amyloid Beta Conformational Seeding Assay
Melting Curves of Triolein Polymorphs
Loss of TREM2 function increases amyloid seeding but reduces plaque-associated ApoE
Amyloid seeding as a disease mechanism and treatment target in transthyretin cardiac amyloidosis
Manual and automatic assignment of two different Aβ40 amyloid fibril polymorphs using MAS solid-state NMR spectroscopy
Maturation-dependent changes in the size, structure and seeding capacity of Aβ42 amyloid fibrils
Amyloid pathology arrangements in Alzheimer’s disease brains modulate in vivo seeding capability
Mechanism of Cellular Formation and In Vivo Seeding Effects of Hexameric β-Amyloid Assemblies
Cryo-EM analysis of the effect of seeding with brain-derived Aβ amyloid fibrils
Hierarchical Protofilament Intertwining Rules the Formation of Mixed‐Curvature Amyloid Polymorphs
Hsp70-mediated disaggregation of α-synuclein amyloid polymorphs
Dissecting aggregation and seeding dynamics of α-Syn polymorphs using the phasor approach to FLIM
Amplification of Brain Aggregated-Amyloid Beta by developing an Amyloid Beta Conformational Seeding Assay
Melting Curves of Triolein Polymorphs
Loss of TREM2 function increases amyloid seeding but reduces plaque-associated ApoE
Amyloid seeding as a disease mechanism and treatment target in transthyretin cardiac amyloidosis
Manual and automatic assignment of two different Aβ40 amyloid fibril polymorphs using MAS solid-state NMR spectroscopy
Maturation-dependent changes in the size, structure and seeding capacity of Aβ42 amyloid fibrils
Amyloid pathology arrangements in Alzheimer’s disease brains modulate in vivo seeding capability
Mechanism of Cellular Formation and In Vivo Seeding Effects of Hexameric β-Amyloid Assemblies