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De novo design of protein binders to stabilize monomeric TDP-43 and inhibit its pathological aggregation

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Protein binders reduce TDP-43 amyloid aggregation in cells, suggesting potential for ALS and FTLD therapy.

The designed protein binders effectively reduced TDP-43 amyloid aggregation in vitro and in cells.
NMR and mutagenesis studies were used to characterize the binding mechanism of the proteins.
The strategy yielded proteins capable of stabilizing TDP-43 with nanomolar binding affinity.
This work provides insights into therapeutic approaches for neurodegenerative diseases like ALS and FTLD.

Sun et al. (2025) studied this question.

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View Full Paper

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Authors

Protein binders reduce TDP-43 amyloid aggregation in cells, suggesting potential for ALS and FTLD therapy.

The designed protein binders effectively reduced TDP-43 amyloid aggregation in vitro and in cells.
NMR and mutagenesis studies were used to characterize the binding mechanism of the proteins.
The strategy yielded proteins capable of stabilizing TDP-43 with nanomolar binding affinity.
This work provides insights into therapeutic approaches for neurodegenerative diseases like ALS and FTLD.

Sun et al. (2025) studied this question.

View Full Paper

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Bookmark