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Modulating Transthyretin Fibril Stability with D-Retro-Inverso Peptides

Coleman, L. M.; Hansmann, U. H. E.

2026-08-18 biophysics
10.64898/2026.08.12.744519 bioRxiv
Show abstract

A major cause of heart failure in elderly patients are deposits of Transthyretin (TTR) fibrils. Using molecular dynamic simulations, we explore how the stability of TTR fibrils can be modulated by D-Retro-Inverso (DRI) Peptides, built from D-amino acids with the sequence of the parent peptide switched, and describe a mechanism by which one of these peptides, DRI-K6V, disrupts TTR fibrils. Our results may open the way to design of peptide drugs targeting established TTR amyloidosis.

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