ArticleScientific reports2015
Self-assembled amyloid fibrils with controllable conformational heterogeneity.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 41 citations in OpenAlex.
- Effect of Microwave on Protein Conformations and Enzymatic Reactions.Molecules (Basel, Switzerland) · 2026Review
- Amyloid Formation in Nanoliter Droplets.International journal of molecular sciences · 2022Article
- Different Aggregation Pathways and Structures for Aβ40 and Aβ42 Peptides.Biomolecules · 2021Article
- Article
- Atomic Force Microscopy Analysis of EPPS-Driven Degradation and Reformation of Amyloid-β Aggregates.Journal of Alzheimer's disease reports · 2018Article
- Mechanical Deformation Mechanisms and Properties of Prion Fibrils Probed by Atomistic Simulations.Nanoscale research letters · 2017Article
- Nanoscale Control of Amyloid Self-Assembly Using Protein Phase Transfer by Host-Guest Chemistry.Scientific reports · 2017Article
- Measurement of amyloid formation by turbidity assay-seeing through the cloud.Biophysical reviews · 2016Review
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid fibrils are a hallmark of neurodegenerative diseases and exhibit a conformational diversity that governs their pathological functions. Despite recent findings concerning the pathological role of their conformational diversity, the way in which the heterogeneous conformations of amyloid fibrils can be formed has remained elusive. Here, we show that microwave-assisted chemistry affects the self-assembly process of amyloid fibril formation, which results in their conformational heterogeneity. In particular, microwave-assisted chemistry allows for delicate control of the thermodynamics of the self-assembly process, which enabled us to tune the molecular structure of β-lactoglobulin amyloid fibrils. The heterogeneous conformations of amyloid fibrils, which can be tuned with microwave-assisted chemistry, are attributed to the microwave-driven thermal energy affecting the electrostatic interaction during the self-assembly process. Our study demonstrates how microwave-assisted chemistry can be used to gain insight into the origin of conformational heterogeneity of amyloid fibrils as well as the design principles showing how the molecular structures of amyloid fibrils can be controlled.
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