Mechanism of amyloid fibril formation triggered by breakdown of supersaturation

Varying methods have been created to amplify amyloid fibrils using mechanical stresses such as agitation, fluid flow or ultrasonication. In addition, numerous studies have revealed the effects of various kinds of additives on amyloid formation focusing on solvation or macromolecular crowding. This review addresses the mechanism of amyloid formation from the viewpoint of supersaturation- and solubility-limited protein phase transition and development of equipment to induce amyloid formation.

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Publication Details

Journal
npj Biosensing
Published
2025-02-03
DOI
https://doi.org/10.1038/s44328-025-00028-z
Citations
8
Primary Topic
Prion Diseases and Protein Misfolding
Type
article
Field-Weighted Citation Impact
6.45

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article

Mechanism of amyloid fibril formation triggered by breakdown of supersaturation

Yuji Goto, Hirotsugu Ogi, Kichitaro Nakajima, Keiichi Yamaguchi
8 citations
npj Biosensing
Prion Diseases and Protein Misfolding
6.45
article

Mechanism of amyloid fibril formation triggered by breakdown of supersaturation

Yuji Goto, Hirotsugu Ogi, Kichitaro Nakajima, Keiichi Yamaguchi
article en
8 citations

Abstract

Varying methods have been created to amplify amyloid fibrils using mechanical stresses such as agitation, fluid flow or ultrasonication. In addition, numerous studies have revealed the effects of various kinds of additives on amyloid formation focusing on solvation or macromolecular crowding. This review addresses the mechanism of amyloid formation from the viewpoint of supersaturation- and solubility-limited protein phase transition and development of equipment to induce amyloid formation.

npj BiosensingVol. 2(1)
The University of Osaka (JP)
Japan Society for the Promotion of Science, Institute for Protein Research, Osaka University
Openalex Percentile: Top 3%
Prion Diseases and Protein Misfolding
6.45
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