Amyloid Depletion

Clearing Pathologic Proteins Across Organs and Diseases

Selectively targeting misfolded or aggregated forms of proteins is a central goal in Neurimmune’s human antibody research and drug development.

Pathologic proteins

Protein aggregation diseases are characterized by misfolding and aggregation of endogenous proteins in affected tissues such as the brain or the heart. During misfolding and aggregation, the affected protein often loses its normal function, becomes more resistant to degradation, and often acquires toxic functions that can cause organ damage.

Human antibodies labelling amyloid for immune-mediated clearance

Amyloid Depletion

Neurimmune develops human antibody therapeutics - so-called ‘depleters’ - that selectively target pathological proteins while sparing normal physiological forms of the proteins, thereby preserving essential biological functions and minimizing the potential for unwanted effects. Upon administration, these antibodies bind their cognate targets and label the pathological proteins for destruction by immune cells through a process known as immune-mediated phagocytosis.

Depletion of misfolded protein aggregates by human antibodies can reduce toxic and mechanical tissue damage, halt disease progression, and allow for recovery, restructuring and regeneration of affected organs. This new therapeutic mechanism may thereby improve long-term outcome and quality of life of patients with protein aggregation diseases.

Christoph Hock, CMO