ArticleNPJ microgravity2020
Characterization of amyloid β fibril formation under microgravity conditions.
Article in NPJ microgravity, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Crystallization for Manufacturing in Microgravity; Are We There Yet?Crystal growth & design · 2026Article
- Time-averaged simulated microgravity ameliorates tau-induced deficit in Drosophila melanogaster.NPJ microgravity · 2026Article
- Physics of Protein Aggregation in Normal and Accelerated Brain Aging.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Microgravity-Assisted Exploration of the Conformational Space of Amyloid β Affected by Tottori-Type Familial Mutation D7N.ACS chemical neuroscience · 2025Article
- Elucidating the Unique J-Shaped Protomer Structure of Amyloid-β(1-40) Fibril with Cryo-Electron Microscopy.International journal of molecular sciences · 2025Article
- Single-Molecule Kinetic Observation of Antibody Interactions with Growing Amyloid β Fibrils.Journal of the American Chemical Society · 2024Article
- Advanced computational approaches to understand protein aggregation.Biophysics reviews · 2024Review
- Changes in interstitial fluid flow, mass transport and the bone cell response in microgravity and normogravity.Bone research · 2022Review
- Conformational Variability of Amyloid-β and the Morphological Diversity of Its Aggregates.Molecules (Basel, Switzerland) · 2022Review
- Fibroblast Differentiation and Matrix Remodeling Impaired under Simulated Microgravity in 3D Cell Culture Model.International journal of molecular sciences · 2021Article
- Cold Atmospheric Plasma Modification of Amyloid β.International journal of molecular sciences · 2021Article
- Protein aggregation: in silico algorithms and applications.Biophysical reviews · 2021Review
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid fibrils are self-assembled and ordered proteinaceous supramolecules structurally characterized by the cross-β spine. Amyloid formation is known to be related to various diseases typified by neurogenerative disorders and involved in a variety of functional roles. Whereas common mechanisms for amyloid formation have been postulated across diverse systems, the mesoscopic morphology of the fibrils is significantly affected by the type of solution condition in which it grows. Amyloid formation is also thought to share a phenomenological similarity with protein crystallization. Although many studies have demonstrated the effect of gravity on protein crystallization, its effect on amyloid formation has not been reported. In this study, we conducted an experiment at the International Space Station (ISS) to characterize fibril formation of 40-residue amyloid β (Aβ(1-40)) under microgravity conditions. Our comparative analyses revealed that the Aβ(1-40) fibrilization progresses much more slowly on the ISS than on the ground, similarly to protein crystallization. Furthermore, microgravity promoted the formation of distinct morphologies of Aβ(1-40) fibrils. Our findings demonstrate that the ISS provides an ideal experimental environment for detailed investigations of amyloid formation mechanisms by eliminating the conventionally uncontrollable factors derived from gravity.
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