Transthyretin amyloidosis is a systemic, progressive disease caused by the dissociation, misfolding, and aggregation of transthyretin (TTR), resulting in extracellular deposition of amyloid fibrils in tissue and organs.

The TTR kinetic stabilizers tafamidis and acoramidis are small molecules that bind to the unoccupied thyroid hormone binding sites of native tetrameric TTR, slowing dissociation and preventing subsequent aggregation.

In randomized controlled clinical trials, tafamidis and acoramidis have significantly reduced cardiomyopathy progression and improved quality of life in patients with transthyretin amyloid cardiomyopathy.

Tafamidis has accumulated long-term clinical trial and real-world evidence supporting its safety, tolerability, and effectiveness; long-term data on acoramidis are still emerging from ongoing clinical trials and real-world use.

Studies employing a subunit exchange assay have not found significant differences in biochemical binding and potency between tafamidis and acoramidis at the plasma concentrations achieved by their standard dosages, despite claims that acoramidis is a more potent TTR kinetic stabilizer.