Our Pipeline
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Indication 1: ATTR Cardiomyopathy (ATTR-CM)
A first-in-class therapeutic antibody engineered to combat transthyretin amyloidosis at the source. It binds selectively to misfolded and aggregated TTR while sparing the normal protein. In preclinical models, it cleared cardiac amyloid deposits and improved cardiac function.
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Stage: Preclinical
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A monoclonal antibody designed to recognize and bind misfolded transthyretin in ATTR polyneuropathy. It neutralizes toxic oligomers and amyloid fibrils while promoting clearance through innate immune cells. In preclinical models, it reduced amyloid in nerves, protected neurons, and improved neurological function.
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Stage: Preclinical
Indication 2:
ATTR Plyneuropathy
(ATTR-PN)
Pipeline by Disease
ATTR Cardiomyopathy
ATTR cardiomyopathy (ATTR-CM) is a progressive and often fatal disease caused by the misfolding and deposition of transthyretin (TTR) protein in the heart muscle. Amyloid fibrils accumulate within the myocardium, leading to stiffening of the heart walls, impaired ventricular filling, and eventually heart failure. Patients typically present with shortness of breath, fatigue, arrhythmias, and reduced exercise tolerance.
I
Indication 1: ATTR Cardiomyopathy (ATTR-CM)
A first-in-class therapeutic antibody engineered to combat transthyretin amyloidosis at the source. It binds selectively to misfolded and aggregated TTR while sparing the normal protein. In preclinical models, it cleared cardiac amyloid deposits and improved cardiac function.
​​
​​
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Stage: Preclinical
Disease Prevalence and Impact
It is estimated that tens of thousands of patients in the U.S. and Europe are affected by ATTR-CM, with both hereditary and wild-type forms contributing to the burden of disease. The condition is frequently underdiagnosed, especially in older adults where symptoms may overlap with other causes of heart failure. Median survival after diagnosis is often only 2–5 years, highlighting the urgent need for disease-modifying therapies. Current treatment options, such as TTR stabilizers or gene silencers, can slow disease progression but do not address the toxic amyloid deposits already present in the heart.
Current Treatment Landscape
No approved therapies directly clear cardiac amyloid. Patients continue to experience disease progression despite available therapies, with significant morbidity, hospitalizations, and high mortality. There remains a critical unmet need for approaches that not only stabilize TTR but also remove existing amyloid deposits to restore cardiac function.
ATTR Polyneuropathy
ATTR polyneuropathy (ATTR-PN) is caused by the same underlying process of misfolded TTR aggregation, but the amyloid deposits primarily infiltrate the peripheral nerves. Progressive amyloid accumulation damages nerve fibers, leading to debilitating symptoms such as pain, numbness, weakness, and impaired motor and sensory function. Patients often experience significant disability and reduced quality of life as the disease advances.
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Indication 2:
ATTR Plyneuropathy
(ATTR-PN)
A monoclonal antibody designed to recognize and bind misfolded transthyretin in ATTR polyneuropathy. It neutralizes toxic oligomers and amyloid fibrils while promoting clearance through innate immune cells. In preclinical models, it reduced amyloid in nerves, protected neurons, and improved neurological function.
​​​
Stage: Preclinical
Disease Prevalence and Impact
ATTR-PN is a rare but severe condition, often manifesting in patients with hereditary TTR mutations. It is estimated that thousands of patients worldwide are affected, with higher prevalence in certain endemic regions (e.g., Portugal, Japan, Sweden). If untreated, ATTR-PN leads to progressive loss of mobility, autonomic dysfunction, and eventually death, with a median survival of less than 10 years after symptom onset.
Current Treatment Landscape
Existing therapies, including gene silencers and stabilizers, may slow the progression of nerve damage but do not directly remove amyloid deposits from affected tissues. Many patients continue to suffer from worsening neuropathy despite treatment. There is an urgent need for disease-modifying therapies that can clear TTR amyloid from the nerves, protect neurons from further damage, and restore neurological function.