Metastasis constitutes the major cause of death in patients with solid tumors. Recently, 16q23 genomic gain was selectively associated with bone metastasis risk in early–stage breast cancer (BCa) and MAF encoded within this region selectively mediated BCa metastasis to bone. As MAF is a transcription factor and therefore a difficult target, we set out to determine whether is possible to identify targetable membrane proteins that are downstream of MAF, to uncover potential metastasis drivers. This led us to the design of random peptide libraries on beads, that upon incubation with cells are able to selectively bind them. The OBOC libraries were synthesized on TentaGel beads, using the split-and-mix method and characterized by UPLC-MS. These libraries were incubated with cells labeled with endogenous fluorophores such as RFP. After the designed library was shown to be successful for interaction with the MCF-7 parental cell line using fluorescence microscopy, the ability to separate positive hits by flow cytometry was explored. Following this it was investigated whether the liquid chromatography coupled to mass spectrometry was a valid method to deconvolute the peptide sequences involved with cell membrane interactions. It was observed that this step is challenging as the pentapeptide libraries used have small masses, more difficult to analyze. Being based on all D-stereoisomers these systems have the advantage of being protease resistant and can be used as potential inhibitors or targeting moieties for metastasis therapy. When tested in breast cancer cell lines, the interaction shows that binding occurs and immunoprecipitation was chosen to validate the potential receptor binding. A successful outcome of this project would lead to identifying new targetable mechanisms for metastasis treatment, where the dissemination rather than growing metastasis could be targeted. This would open up new possibilities in increasing the overall efficiency of the existing cancer therapy.