Platinum complex drugs such as cisplatin have been used as highly successful chemotherapy drugs since the 1970s. We are interested in how the ligands attached to cisplatin analogs influences their reactivity with biologically relevant targets along with time and amount. For this study, reactions were conducted to determine the reactivity between different platinum compounds and the protein bovine serum albumin. Various platinum compounds with different ligands were reacted in varying amounts with albumin in ammonium acetate buffer for either 1 hour, 4 hours, or 24 hours. Each reaction was quenched after the designated reaction time by dialysis and the platinum bound to the protein was determined by use of ICP. LC-MS was used to find exact peptide residues platinum complexes prefer to bind with but was found to be ineffective. Results show that time has a more significant affect on binding over amount of platinum present. In respect to changing the leaving or carrier ligands on the platinum complex, these changes on the complex did not affect binding significantly with bovine serum albumin. Triamine platinum complexes also seem to bind significantly more than diamine platinum complexes along with anionic form platinum complexes binding significantly better than the cationic form platinum complexes.