The aim of my research is the design, synthesis and characterization of amphipathic helical peptide inhibitors (AHPs), which target the TDP-43-membrane interaction. TDP-43 is an aggregation prone protein with a high association propensity towards membrane surfaces. Mutations in TDP 43 result in formation of insoluble aggregates and proteinaceous inclusions upon membrane association. These inclusions are found in many neurodegenerative diseases, e.g. amyotrophic lateral sclerosis (ALS). This interaction was reported to be crucial for the aggregation process of TDP 43 and its pathological mutants. AHPs are tested for their inhibitory potential using CD spectroscopy, FRET- and colorimetric assays on labelled membranes, RIfS and the Thioflavin T assay.