Protein Aggregation Diseases

Protein aggregation diseases include Alzheimer’s and Parkinson’s diseases, amyotrophic lateral sclerosis, dementia with Lewy bodies, frontotemporal dementia and Huntington’s disease. Moreover, amyloid transthyretin cardiomyopathy and type-2 diabetes are increasingly recognized as protein aggregation diseases.

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.

Endogenous proteins prone to misfolding and aggregation include amyloid beta, tau, alpha-synuclein, TAR DNA binding protein 43, C9orf72 related proteins, islet amyloid polypeptide and transthyretin.

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

With Neurimmune's scientific approach, the normal physiological forms of these proteins with important biological functions remain unaffected, reducing the potential for unwanted effects. Together with their human origin and optimization guided by the principles of the human immune system, these selectivities provide for the favorable profiles in clinical trials.