ProMIS Neurosciences Inc. announced the publication of supportive preclinical data in the Journal of Biological Chemistry in an article titled, "Tryptophan residues in TDP-43 and SOD1 modulate the cross-seeding and toxicity of SOD1. ALS is a fatal neurodegenerative disease of motor neurons.oxic aggregates of superoxide dismutase-1 (SOD1) and TAR DNA-binding protein 43 (TDP-43) in motor neurons are characteristic of ALS. The study showed that these two proteins interact such that misfolding of TDP-43 leads to misfolding and aggregation of SOD1 in a cell system and promotes motor neuron damage in zebrafish.

The study demonstrated a pathologic synergy between SOD1 and TDP-43 in cell culture and in zebra fish. The interaction between these 2 proteins was characterized at the molecular level. The results indicated that the misfolding TDP-43 epitope previously identified by ProMIS and targeted by PMN267 contains a tryptophan amino acid critical to the pathogenic interaction with SOD1 thereby providing further biological support for the potential of therapeutic intervention with PMN267.