The current standard of care for GM2 Gangliosidosis disease is limited to supportive care and aimed at providing adequate nutrition and hydration.This supportive care may substantially improve the quality of life of people affected by GM2. The therapeutic team may include specialists in neurology, pulmonology, gastroenterology, psychiatrist, orthopaedics, nutrition, physical therapy and occupational therapy. N-Acetyl-Leucine
N-Acetyl-Leucine is an orally administered, modified amino acid that is being developed as a novel treatment for multiple rare and common neurological disorders by IntraBio Inc (Oxford, United Kingdom).N-Acetyl-Leucine has been granted multiple orphan drug designations from the U.S. Food & Drug Administration (FDA)  and the European Medicines Agency (EMA) and the European Medicines Agency (EMA) for the treatment of a various genetic diseases, including GM2 Gangliosidosis (Tay-Sachs and Sandhoff). The US FDA has granted IntraBio a Rare Pediatric Disease Designation for N-Acetyl-Leucine for the treatment of GM2 Gangliosidosis.Compassionate use studies in both Tay-Sachs and Sandhoff patients have demonstrated the positive clinical effects of treatment with N-Acetyl-Leucine for GM2 Gangliosidosis  These studies further demonstrated that the treatment is well tolerated, with a good safety profile.A multinational clinical trial investigating N-Acetyl-L-Leucine for the treatment of GM2 Gangliosidosis (Tay-Sachs and Sandhoff) began in 2019 Recruitment is ongoing. IntraBio is also conducting parallel clinical trials with N-Acetyl-L-Leucine for the treatment of Niemann-Pick disease type C and Ataxia-Telangiectasia. Future opportunities to develop N-Acetyl-Leucine include Lewy body dementia, amyotrophic lateral sclerosis, restless leg syndrome, multiple sclerosis, and migraine. See also
GM2 (ganglioside)

References
External links
GeneReview/NIH/UW entry on Hexosaminidase A Deficiency
With a prion, two protein chains are stabilized if one binds to another in the same conformation. The probability of this happening is low, but once it does the combination of the two is very stable. Then more units can get added, making a sort of "fibril". Prions form abnormal aggregates of proteins called amyloids, which accumulate in infected tissue and are associated with tissue damage and cell death. Amyloids are also responsible for several other neurodegenerative diseases such as Alzheimers disease and Parkinsons disease.A prion disease is a type of proteopathy, or disease of structurally abnormal proteins. In humans, prions are believed to be the cause of Creutzfeldt–Jakob disease (CJD), its variant (vCJD), Gerstmann–Sträussler–Scheinker syndrome (GSS), fatal familial insomnia (FFI), and kuru. There is also evidence suggesting prions may play a part in the process of Alzheimers disease, Parkinsons disease, and amyotrophic lateral sclerosis (ALS); these have been termed prion-like diseases. Several yeast proteins have also been identified as having prionogenic properties, as well as a protein involved in modification of synapses during the formation of memories (see Eric Kandel § Molecular changes during learning). Prion replication is subject to epimutation and natural selection just as for other forms of replication, and their structure varies slightly between species.Prion aggregates are stable, and this structural stability means that prions are resistant to denaturation by chemical and physical agents: they cannot be destroyed by ordinary disinfection or cooking. This makes disposal and containment of these particles difficult.