Open hardware in microscopy

Hohlbein, Johannes; Faez, Sanli

doi:10.1016/j.ohx.2023.e00473

Cited by 2 publications

(1 citation statement)

References 30 publications

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“…9405020) were used without any intense pipetting of the droplet suspension. Single-molecule fluorescence microscopy imaging of such samples was performed using a home-built super-resolution microscope – the miEye 45,46 . To visualize the individual glass surface-attached α-syn droplets, TIRF microscopy was employed 47 , whereas imaging of larger α-syn formations, such as droplet aggregates, was conducted under HILO illumination.…”

Section: Methodsmentioning

confidence: 99%

Liquid-liquid Phase Separation of Alpha-synuclein Increases the Structural Variability of Fibrils Formed during Amyloid Aggregation

Ziaunys,

Sulskis,

Veiveris

et al. 2023

Preprint

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Protein liquid-liquid phase separation (LLPS) is a rapidly emerging field of study on biomolecular condensate formation. In recent years, this phenomenon has been implicated in the process of amyloid fibril formation, serving as an intermediate step between the native protein transition into their aggregated state. The formation of fibrils via LLPS has been demonstrated for a number of proteins related to neurodegenerative disorders, as well as other amyloidoses. Despite the surge in amyloid-related LLPS studies, the influence of protein condensate formation on the end-point fibril characteristics is still far from fully understood. In this work, we compare alpha-synuclein aggregation under conditions, which promote or negate its LLPS and examine the differences between the formed aggregates. We show that alpha-synuclein phase separation generates a wide variety of assemblies with distinct secondary structures and morphologies. The LLPS-induced structures also possess higher levels of toxicity to cells, indicating that biomolecular condensate formation may be a critical step in the appearance of disease-related fibril variants.

show abstract

Section: Methodsmentioning

confidence: 99%

Liquid-liquid Phase Separation of Alpha-synuclein Increases the Structural Variability of Fibrils Formed during Amyloid Aggregation

Ziaunys,

Sulskis,

Veiveris

et al. 2023

Preprint

View full text Add to dashboard Cite

show abstract

Liquid–liquid phase separation of alpha‐synuclein increases the structural variability of fibrils formed during amyloid aggregation

Ziaunys,

Sulskis,

Veiveris

et al. 2024

The FEBS Journal

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Protein liquid–liquid phase separation (LLPS) is a rapidly emerging field of study on biomolecular condensate formation. In recent years, this phenomenon has been implicated in the process of amyloid fibril formation, serving as an intermediate step between the native protein transition into their aggregated state. The formation of fibrils via LLPS has been demonstrated for a number of proteins related to neurodegenerative disorders, as well as other amyloidoses. Despite the surge in amyloid‐related LLPS studies, the influence of protein condensate formation on the end‐point fibril characteristics is still far from fully understood. In this work, we compare alpha‐synuclein aggregation under different conditions, which promote or negate its LLPS and examine the differences between the formed aggregates. We show that alpha‐synuclein phase separation generates a wide variety of assemblies with distinct secondary structures and morphologies. The LLPS‐induced structures also possess higher levels of toxicity to cells, indicating that biomolecular condensate formation may be a critical step in the appearance of disease‐related fibril variants.

show abstract

Open hardware in microscopy

Cited by 2 publications

References 30 publications

Liquid-liquid Phase Separation of Alpha-synuclein Increases the Structural Variability of Fibrils Formed during Amyloid Aggregation

Liquid-liquid Phase Separation of Alpha-synuclein Increases the Structural Variability of Fibrils Formed during Amyloid Aggregation

Liquid–liquid phase separation of alpha‐synuclein increases the structural variability of fibrils formed during amyloid aggregation

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