Enhanced in vitro aggregation, but not phase separation, of TDP-43 and its C-terminal fragments generate intrinsic deep-blue autofluorescence.

Preethi Saravanan; Vidhya Bharathi; Priyadarshini Veerabhadraswamy; Basant K. Patel

doi:10.1039/d5nj02842f

January 1, 2025New Journal of Chemistry

Enhanced in vitro aggregation, but not phase separation, of TDP-43 and its C-terminal fragments generate intrinsic deep-blue autofluorescence.

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Key Points

Enhanced aggregation of TDP-43 fragments leads to intrinsic deep-blue autofluorescence, indicating potential diagnostic use.
Strong evidence reveals that aggregation, not phase separation, contributes to TDP-43's fluorescence behavior.
The analysis employed in vitro experimental methods to explore TDP-43's role in proteinopathies like ALS.
This work suggests that further investigations are needed to clarify the mechanisms of TDP-43 in disease states.

Implication

Research shows enhanced aggregation of TDP-43 fragments, indicating their role in proteinopathies like ALS.

Abstract

As misfolding, phase-separation and aggregation of the RNA/DNA-binding protein, TDP-43, are implicated to proteinopathies like ALS, condensate-type distinction is important for mechanistic elucidation and therapeutic targeting. Here, we examined if...

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Cite This Study

Saravanan et al. (2025) studied this question.

synapsesocial.com/papers/68af53ffad7bf08b1eadaa4e https://doi.org/10.1039/d5nj02842f

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Enhanced in vitro aggregation, but not phase separation, of TDP-43 and its C-terminal fragments generate intrinsic deep-blue autofluorescence.

Key Points

Implication

Abstract

Discussion

Cite This Study

Enhanced in vitro aggregation, but not phase separation, of TDP-43 and its C-terminal fragments generate intrinsic deep-blue autofluorescence.

Key Points

Implication

Abstract

Discussion

Cite This Study

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