ArticleThe Journal of biological chemistry2025
Mechanism of inhibition of acid-mediated transthyretin aggregation by designed peptides.
Article in The Journal of biological chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Aggregation of transthyretin (TTR) causes TTR cardiomyopathy and polyneuropathy through amyloidosis. To initialize TTR aggregation, the native TTR tetramer first dissociates to a monomeric intermediate, which misfolds and self-assembles to oligomers, eventually forming insoluble aggregates and fibrils. Peptide inhibitors have been designed to cap two β-strands that are buried in the well-folded tetramer but are solvent-exposed in the monomeric aggregation intermediate. However, how these peptides affect the reaction kinetics of individual steps in the multi-step TTR aggregation pathway remains unknown. Here, we integrated
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