ALS treatments that currently are being used under FDA approval have a level that relieves symptoms and slows the progression of Lou Gehrig. Deargen is challenging the development of new ALS treatments by reducing TDP-43 protein aggregation observed in more than 90% of patients with Lou Gehrig.
Lou Gehrig is the name of a famous baseball player in the major leagues of the 1930s. As he has died of amyotrophic lateral sclerosis that muscles lose strength as muscle neurons are gradually destroyed during his career, it was named Lou Gehrig’s disease. Lou Gehrig is a rare, neurodegenerative and intractable disease that affects 100,000 people worldwide and about 3000 patients in our country (as of 2015).
ALS is a disease in which muscle nerve cells are destroyed and muscles gradually lose strength. It becomes difficult to eat or express language as the movements of the hands and legs begin to dull, the paralysis of muscles gradually increases. Eventually, it causes death due to breathing problems.
The exact cause of this ALS disease is unknown. It is estimated that about 10% of the patients are genetic, and the remaining 90% are due to immunity, oxidative toxicity, excitatory toxicity, environmental factors and protein aggregation, etc. Among these, an aggregated TDP-43 protein has been observed in more than 90% of patients with ALS, and many studies have reported that this may be an important cause of Lou Gehrig’s disease.
Therapeutics that currently are being used under FDA are Rilutek (riluzole tablet), Tiglutik (riluzole suspension), Radicava (edaravone), etc. Each of these drugs shows only the effects of reducing the symptoms and slowing the progression, not the radical treatment of ALS. Therefore, there is an urgent need to develop a cure for treating ALS fundamentally.
We want to contribute to the fight against ALS by developing a drug that can reduce the aggregation of TDP-43 protein. Currently, we have a system for evaluating the efficacy of drugs by observing the decrease in TDP-43 aggregation with images. By using this, we are discovering small molecules that can control abnormal aggregation of TDP-43 with the DTI (drug target interaction) algorithm developed by us.
By establishing a partnership with Dankook University, we are currently validating the efficacy of the discovered small molecules at the non-clinical stage.
 Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis. DOI: 10.1126/science.1134108
 TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis DOI: 10.1126/science.1154584