Interactions between proteins are important throughout life. Proteins are able to combine many weak interactions to create strong and specific interactions between each other. However, predicting how, and if proteins interact from their sequence remains elusive. This ability would be crucial as we have collected swaths of sequencing data during the last two decades as nextgeneration sequencing machines have revolutionized genomics. These next-generations sequencing machines are good at measuring enormous amounts of sequences in parallel. This technology can also be used to perform high-throughput biochemical measurements, as first demonstrated by the Hits-FLIP method, which was applied to measure transcription factor binding to DNA. This report aims to develop this method further, inspired by the PICASSO method that demonstrated a way to attach proteins to a DNA-microarray in a controlled manner using CRISPR-technology. The method we aim to develop will use the illumina sequencing platform and a TIRF microscope to investigate the interactions between proteins and peptides. The proteins of interest will be fused to dCas9 and tagged with a fluorophore, interactions will be detected using FRET. In this project we have designed and produced such fusion proteins and demonstrated that they can bind specifically to the correct barcode sequence and be tagged with fluorophores. The next step will be to further optimize the design and to perform measurements on a TIRF microscope.