ArticleProceedings of the National Academy of Sciences of the United States of America2015
Force generation by the growth of amyloid aggregates.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Attonewton Force Resolution Measurements with Silicon Nanospheres at the Thermal Noise Limit in Ambient-Temperature Liquids.Nano letters · 2025Article
- Mimicking Kidney Flow Shear Efficiently Induces Aggregation of LECT2, a Protein Involved in Renal Amyloidosis.bioRxiv : the preprint server for biology · 2023Article
- Enhancing Protein Crystal Nucleation Using In Situ Templating on Bioconjugate-Functionalized Nanoparticles and Machine Learning.ACS applied materials & interfaces · 2023Article
- Stability matters, too - the thermodynamics of amyloid fibril formation.Chemical science · 2022Review
- Deciphering the Structure and Formation of Amyloids in Neurodegenerative Diseases With Chemical Biology Tools.Frontiers in chemistry · 2022Review
- Liquid-Liquid Phase-Separated Systems from Reversible Gel-Sol Transition of Protein Microgels.Advanced materials (Deerfield Beach, Fla.) · 2021Article
- From Protein Building Blocks to Functional Materials.ACS nano · 2021Review
- Bioinspired Suprahelical Frameworks as Scaffolds for Artificial Photosynthesis.ACS applied materials & interfaces · 2020Article
- Systematic Investigation of Insulin Fibrillation on a Chip.Molecules (Basel, Switzerland) · 2020Article
- Microfluidics for real-time direct monitoring of self- and co-assembly biomolecular processes.Nanotechnology · 2019Review
- Article
- A minimal conformational switching-dependent model for amyloid self-assembly.Scientific reports · 2016Article
- Amyloid persistence in decellularized liver: biochemical and histopathological characterization.Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis · 2016Article
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
The generation of mechanical forces are central to a wide range of vital biological processes, including the function of the cytoskeleton. Although the forces emerging from the polymerization of native proteins have been studied in detail, the potential for force generation by aberrant protein polymerization has not yet been explored. Here, we show that the growth of amyloid fibrils, archetypical aberrant protein polymers, is capable of unleashing mechanical forces on the piconewton scale for individual filaments. We apply microfluidic techniques to measure the forces released by amyloid growth for two systems: insulin and lysozyme. The level of force measured for amyloid growth in both systems is comparable to that observed for actin and tubulin, systems that have evolved to generate force during their native functions and, unlike amyloid growth, rely on the input of external energy in the form of nucleotide hydrolysis for maximum force generation. Furthermore, we find that the power density released from growing amyloid fibrils is comparable to that of high-performance synthetic polymer actuators. These findings highlight the potential of amyloid structures as active materials and shed light on the criteria for regulation and reversibility that guide molecular evolution of functional polymers.
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