Complete aggregation pathway of amyloid ß (1-40) and (1-42) resolved on an atomically clean interface.
Sci Adv
; 6(15): eaaz6014, 2020 04.
Article
em En
| MEDLINE
| ID: mdl-32285004
ABSTRACT
To visualize amyloid ß (Aß) aggregates requires an uncontaminated and artifact-free interface. This paper demonstrates the interface between graphene and pure water (verified to be atomically clean using tunneling microscopy) as an ideal platform for resolving size, shape, and morphology (measured by atomic force microscopy) of Aß-40 and Aß-42 peptide assemblies from 0.5 to 150 hours at a 5-hour time interval with single-particle resolution. After confirming faster aggregation of Aß-42 in comparison to Aß-40, a stable set of oligomers with a diameter distribution of ~7 to 9 nm was prevalently observed uniquely for Aß-42 even after fibril appearance. The interaction energies between a distinct class of amyloid aggregates (dodecamers) and graphene was then quantified using molecular dynamics simulations. Last, differences in Aß-40 and Aß-42 networks were resolved, wherein only Aß-42 fibrils were aligned through lateral interactions over micrometer-scale lengths, a property that could be exploited in the design of biofunctional materials.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptídeos beta-Amiloides
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Microscopia de Força Atômica
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Simulação de Dinâmica Molecular
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Agregação Patológica de Proteínas
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Agregados Proteicos
Idioma:
En
Ano de publicação:
2020
Tipo de documento:
Article