My work focuses on the design, synthesis and biophysical investigation of small organic molecules that have the potential to stabilize the SOD1 homodimer. SOD1 is a protein that is prone to aggregation via several different pathways with one including mutation-induced dissociation of the homodimeric structure into instable monomers. These aggregates can be found in 20% of all genetically determined cases of Amyotrophic Lateral Sclerosis (fALS), a fatal neurodegenerative disorder. The specifically designed small molecules are examined for their ability to stabilize the homodimer in an affinity-based targeting process and are envisaged as aggregation inhibitors and sensory molecules for the determination of SOD1 aggregation processes.