• RTM
    Reverse Translational
    Medicine

«We are aiming at making efficacious immunotherapeutics designed to serve patients in need for better, safer, life-saving medicines.»

Roger Nitsch, MD, President

Scientific Background

Protein aggregation diseases including type-2 diabetes and a large variety of neurodegenerative diseases such as Alzheimer’s and Parkinson’s diseases represent the greatest challenges for our aging societies and health care providers alike. As a result of increased life expectancy and improved general prevention, the prevalence of protein aggregation diseases is increasing dramatically. The suffering of a large population of elderly patients along with the daily stress of their caregivers is causing tremendous social and financial challenges for our societies already today, with strongly increasing trends for the coming decades. Scientific progress in understanding the underlying biological principles of protein aggregation diseases allow scientists for the first time to develop highly selective treatments as well as diagnostic procedures designed to target protein aggregation diseases at the source: the pathogenic protein aggregate. Protein aggregate diseases are characterized by the common mechanism of misfolding, aggregation and deposition in the affected tissue or organ of otherwise physiological proteins with important biological functions. During the process of misfolding and aggregation, the affected protein often loses its normal function, becomes more resistant to degradation, accumulates and in many cases acquires toxic functions that ultimately damages the organ affected by the protein aggregates deposition. Protein aggregation diseases include neurological disorders like Alzheimer’s and Parkinson’s diseases, dementia with Lewy bodies, Huntington’s disease, frontotemporal dementia, amyotrophic lateral sclerosis, multiple systems atrophy, progressive supranuclear palsy and Pick’s disease. Among metabolic diseases, type-2 diabetes is increasingly recognized by researches as having protein aggregation pathology in insulin-producing pancreatic islet cells - the failure of which is a major component of the clinical diabetic syndrome. Other examples for protein aggregation diseases include transthyretin (TTR)-related cardiomyopathy and polyneuropathy in which misfolded TTR aggregates accumulate in the affected heart cells and peripheral nerves ultimately causing organ failure.

Selectively targeting the misfolded, pathogenic forms of an aggregated target protein is a central goal in Neurimmune’s antibody research and development efforts in protein aggregation diseases. In these indication areas, the normally folded or physiological forms of these proteins with important biological functions are unaffected by Neurimmune’s antibody approach, thus minimizing the potential for unwanted side effects. Together with their human origin and optimization guided by the principles of the human immune system, these features provide for the favorable safety profiles of Neurimmune’s antibodies seen in clinical trials.