Abstract
Conversion to amyloid-like fibrils and/or aggregation of numerous soluble proteins is associated with several pathologies such as amyotrophic lateral sclerosis (ALS), Alzheimer’s, and Parkinson’s diseases. Cu, Zn-superoxide dismutase (SOD1) is an important anti-oxidative enzyme that protects cells. Mutations of the gene coding for SOD1 cause familial ALS. We found that the self-assembly of amyloid-like fibrils by SOD1 in certain conditions was accompanied by the formation of hydrogels rather than precipitation, notably when the concentration of the protein was sufficiently high. The structure of the hydrogels and pathogenic SOD1 fibrils remains unknown.
