### Learning objectives Systemic amyloidosis is characterised by misfolding of proteins which deposit as insoluble amyloid fibrils in various organs, including the heart. Most cases of cardiac amyloidosis (CA) result from misfolding of immunoglobulin light chains produced by a clonal plasma cell disorder (AL amyloidosis), or transthyretin (TTR) protein produced predominantly in the liver (ATTR amyloidosis). ATTR amyloidosis frequently results from age-related misfolding of the wild-type TTR (ATTRwt), and less commonly, from misfolding of a variant TTR from an autosomal dominant mutation of the TTR gene (ATTRv). The misfolded proteins deposit as insoluble amyloid fibrils in the myocardial interstitial space, disrupting its architecture and causing a prototypical restrictive cardiomyopathy with high mortality. Without treatment, median survival from diagnosis ranges from <6 months for AL-CA to 3–5 years for ATTR-CA.1 Diagnosis is often delayed because of low disease awareness, leading to