Designing polymer–peptide conjugates to target dipeptide repeat aggregates implicated in amyotrophic lateral sclerosis

Vincent P. Gray; Zixian Cui; Mackenzie Klepsig; Rachel A. Letteri

doi:10.1039/d6tb00210b

January 1, 2026Journal of Materials Chemistry BOpen Access

Designing polymer–peptide conjugates to target dipeptide repeat aggregates implicated in amyotrophic lateral sclerosis

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Key Points

This research aims to explore how polymer-peptide conjugates can prevent the aggregation of toxic peptides associated with amyotrophic lateral sclerosis.
Designed polymer-peptide conjugates
Assessed their ability to inhibit aggregation of glycine-alanine dipeptide repeats
Focused on the implications for ALS progression
Polymer-peptide conjugates significantly hindered the aggregation of GA peptides.
Demonstrated a potential therapeutic approach for addressing progression in amyotrophic lateral sclerosis.

Implication

Evaluates polymer-peptide conjugates' effects on dipeptide repeat aggregates in ALS, suggesting new therapeutic approaches.

Abstract

Polymer-peptide conjugates hinder aggregation of the toxic dipeptide repeat glycine–alanine (GA) n peptide that is implicated in the progression of amyotrophic lateral sclerosis, a lethal neuromuscular disease with an urgent need for new therapeutics.

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Cite This Study

Gray et al. (2026) studied this question.

synapsesocial.com/papers/6a323ed9d50b63ecad207f82 https://doi.org/10.1039/d6tb00210b

View Full Paper

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Designing polymer–peptide conjugates to target dipeptide repeat aggregates implicated in amyotrophic lateral sclerosis

Key Points

Implication

Abstract

Discussion

Cite This Study

Designing polymer–peptide conjugates to target dipeptide repeat aggregates implicated in amyotrophic lateral sclerosis

Key Points

Implication

Abstract

Discussion

Cite This Study

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