Amyloid Fibril (Transthyretin)

Amyloid fibrils formed from transthyretin (TTR) are highly ordered, elongated protein aggregates characterized by a cross-β-sheet structure. These fibrils result from the misfolding and aggregation of TTR, a normally soluble transport protein for thyroxine (T4) and retinol-binding protein. Destabilization of the native tetrameric structure leads to dissociation into monomers or dimers, which misfold and self-associate into amyloidogenic intermediates that aggregate into amyloid fibrils. This process underlies diseases such as wild-type transthyretin amyloidosis (wtATTR), familial amyloid polyneuropathy, senile systemic amyloidosis, and cardiac amyloidosis. Therapeutic strategies focus on stabilizing the TTR tetramer to prevent fibril formation.

Other names

TTR AmyloidTransthyretin Amyloid Fibrils

Stabilization of TTR tetramer to prevent dissociation and subsequent amyloid fibril formation.