A naturally occurring right-handed coiled tetramer protein was identified in Staphylothermus marnus, a thermophilic marine organism. Previous research shows that the hydrophobic interactions and network of salt bridges on the surface create an exceedingly stable tetrameric peptide (Stetefeld et al, 2000). Modification of the tetramer sequence was done to include a binding site to inhibit a transmembrane protein that is upregulated in prostate cancer cells. Currently, inhibition of the transmembrane protein, Prostate Specific Membrane Antigen (PSMA), is thought to induce apoptosis through the p38 MAPK pathway (Evans et al, 2016). After expression and purification of the modified tetramer protein, its presence was verified using liquid chromatography and gel electrophoresis. Binding analysis to Glucose-Regulated Protein (GRP) 78 as a non-specific binding measurement control using bio-layer interferometry was done resulting in the expected negative results. Subsequent testing to the target biomarker PSMA using microscale thermophoresis also demonstrated negative results. Further testing using varying concentrations of ligand is necessary in order to establish reliable results.