ArticleProtein science : a publication of the Protein Society2022
In vivo liquid-liquid phase separation protects amyloidogenic and aggregation-prone peptides during overexpression in Escherichia coli.
Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Advances in engineering and applications of synthetic phase-separated membraneless organelles in biotechnology.Synthetic and systems biotechnology · 2026Review
- Engineered membraneless organelles inSynthetic and systems biotechnology · 2025Article
- Cephalopod proteins for bioinspired and sustainable biomaterials design.Materials today. Bio · 2025Review
- Controlling Drug Partitioning in Individual Protein Condensates through Laser-Induced Microscale Phase Transitions.Journal of the American Chemical Society · 2024Article
- Oxidative Stress Induced by Arsenite is Involved in YTHDF2 Phase Separation.Biological trace element research · 2024Article
- Article
- Mass Spectrometry of RNA-Binding Proteins during Liquid-Liquid Phase Separation Reveals Distinct Assembly Mechanisms and Droplet Architectures.Journal of the American Chemical Society · 2023Article
- Release of frustration drives corneal amyloid disaggregation by brain chaperone.Communications biology · 2023Article
- Recombinant protein condensation insideMaterials today. Bio · 2022Article
- In vivo liquid-liquid phase separation protects amyloidogenic and aggregation-prone peptides during overexpression in Escherichia coli.Protein science : a publication of the Protein Society · 2022Article
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Authors and funding
10 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Studying pathogenic effects of amyloids requires homogeneous amyloidogenic peptide samples. Recombinant production of these peptides is challenging due to their susceptibility to aggregation and chemical modifications. Thus, chemical synthesis is primarily used to produce amyloidogenic peptides suitable for high-resolution structural studies. Here, we exploited the shielded environment of protein condensates formed via liquid-liquid phase separation (LLPS) as a protective mechanism against premature aggregation. We designed a fusion protein tag undergoing LLPS in Escherichia coli and linked it to highly amyloidogenic peptides, including β amyloids. We find that the fusion proteins form membraneless organelles during overexpression and remain fluidic-like. We also developed a facile purification method of functional Aβ peptides free of chromatography steps. The strategy exploiting LLPS can be applied to other amyloidogenic, hydrophobic, and repetitive peptides that are otherwise difficult to produce.
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