University of Detroit Mercy Dearborn, Michigan, United States
Reham Alkohaif (University of Detroit Mercy)| Monica Bean (University of Detroit Mercy)| Mara Livezey (University of Detroit Mercy)
Excluding lung cancer, breast cancer death rates among women are higher than any other cancer. BHPI, a small molecule bio-modulator of estrogen receptor (ERα), could be vital in developing life-saving treatment for people living with breast cancer. BHPI activates an endoplasmic reticulum (EnR) stress-response pathway that maintains protein folding homeostasis and quality control. This eventually ends in necrotic cell death, initiated by strong and sustained activation of the anticipatory UPR, killing ERα positive cancer cells. BHPI possibly binds too tightly to ERα, so it has thus far been recalcitrant to crystallography and binding studies. In order to utilize BHPI in breast cancer treatment, it is important to identify its binding site on ERα. Three estrogen receptor PDB structures: 1a52, 3ert, and 5u2b, were studied through computational programs RefineD, PyMOL, and SwissDock. Interactions between a specific amino acid, Leucine 320, and BHPI were studied using these programs to identify and probe possible binding sites. BHPI and leucine appear to have hydrophobic interactions. Future studies are required to indicate additional interactions between Leucine 320 and BHPI.