Abstract: The misfolding and subsequent aggregation of proteins into amyloid fibrils underlie the onset of a variety of human disorders collectively known as amyloidosis. Transthyretin (TTR) is one of the > 30 amyloidogenic proteins identified to date and is associated with a group of highly debilitating and life-threatening disorders called TTR amyloidosis (ATTR). ATTR comprises senile systemic amyloidosis, which is linked to wildtype (WT) TTR aggregation, and hereditary ATTR, a dominantly inherited disorder caused by the deposition of one of over 130 TTR genetic variants. Senile systemic amyloidosis is a prevalent age-related amyloidosis, affecting up to 25% of the population over 80 years of age, and is characterized by the build-up of TTR fibrils in the myocardium. Regarding hereditary ATTR, the clinical presentation is highly heterogeneous, primarily affecting the peripheral nervous system (familial amyloid polyneuropathy – FAP) or the heart (familial amyloid cardiomyopathy). In rare cases, aggregation develops in the central nervous system, giving rise to a phenotype known as familial leptomeningeal amyloidosis (Carroll et al., 2022).