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Molecular mechanism for the synchronized electrostatic coacervation and co-aggregation of alpha-synuclein and tau

Here, the authors report that α-synuclein phase-separates into liquid condensates with positively charged polypeptides such as Tau. The condensates undergo different maturation processes, including the formation of α-synuclein/Tau amyloid hetero-aggregates inside the condensates.

Pablo Gracia
David Polanco
Nunilo Cremades
ResearchOpen Access06 Aug 2022
Nature Communications

Volume: 13, P: 1-16
The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells

The self-assembly of α-synuclein (αS) is a pathological feature of Parkinson’s disease. The αS species responsible for neuronal damage are not well characterized. Here, the authors show that αS fibrils release soluble prefibrillar oligomeric species responsible for neurotoxicity in vitro.

Roberta Cascella
Serene W. Chen
Cristina Cecchi
ResearchOpen Access22 Mar 2021
Nature Communications

Volume: 12, P: 1-16
α-Helical peptidic scaffolds to target α-synuclein toxic species with nanomolar affinity

α-Synuclein (αS) aggregation is a driver of several neurodegenerative disorders. Here, the authors identify a class of peptides that bind toxic αS oligomers and amyloid fibrils but not monomeric functional protein, and prevent further αS aggregation and associated cell damage.

Jaime Santos
Pablo Gracia
Salvador Ventura
ResearchOpen Access18 Jun 2021
Nature Communications

Volume: 12, P: 1-14
Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism

Limbocker et al. show that trodusquemine, an aminosterol, reduces the cytotoxicity of protein misfolded oligomers by displacing them from cell membranes in the absence of any overt structural/ morphological changes in them. This mechanism appears to be general, as they test it for oligomers of αS, Aβ and the model protein HypF-N to human neuroblastoma cells.

Ryan Limbocker
Benedetta Mannini
Christopher M. Dobson
ResearchOpen Access13 Aug 2020
Communications Biology

Volume: 3, P: 1-10
Novel Small Molecules Targeting the Intrinsically Disordered Structural Ensemble of α-Synuclein Protect Against Diverse α-Synuclein Mediated Dysfunctions

Gergely Tóth
Thomas Neumann
Lisa McConlogue
ResearchOpen Access18 Nov 2019
Scientific Reports

Volume: 9, P: 1-14
Single-molecule FRET studies on alpha-synuclein oligomerization of Parkinson’s disease genetically related mutants

Laura Tosatto
Mathew H. Horrocks
David Klenerman
ResearchOpen Access19 Nov 2015
Scientific Reports

Volume: 5, P: 1-12

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Molecular mechanism for the synchronized electrostatic coacervation and co-aggregation of alpha-synuclein and tau

The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells

α-Helical peptidic scaffolds to target α-synuclein toxic species with nanomolar affinity

Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism

Novel Small Molecules Targeting the Intrinsically Disordered Structural Ensemble of α-Synuclein Protect Against Diverse α-Synuclein Mediated Dysfunctions

Single-molecule FRET studies on alpha-synuclein oligomerization of Parkinson’s disease genetically related mutants

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