This was done by subjecting such complexes to tryptic digestion followed by mass spectrometry to assign protein identification, in effect creating AR interactomes initiated by ligand binding. To our MS data, a label-free quantitative method has now been applied across the different experimental paradigms, which allowed us to obtain data related to protein identification, along with abundance, thus allowing for direct comparisons between stimulation conditions. The aim of differential hormone stimulation conditions will allow us to determine whether disease etiology of the T877A-AR mutation is dependent upon ligand and co-factor status. Therefore, we used LNCaP cells that endogenously express the T877AAR mutation to characterize the ligand promiscuous protein interactome complexes under different hormonal conditions, in order to highlight the possible distinct complexes that may be linked to disease progression. LNCaP cells were stimulated with the following hormones, four androgens: DHT, mibolerone, R1881, or testosterone, or 17b-Estradiol, progesterone, dexamethasone, or the anti-androgen cyproterone actetate, alone or with no-ligand/alcohol-vehicle control. Hormone stimulated T877A-AR complexes were immunopurified with an N-terminal specific AR antibody, which would not interfere with hormone binding to the AR ligand-binding domain. Eluates from all experimental conditions were analyzed by LCMS/MS. In order to increase our sample frequency for peptide detection in our MS analysis, each experimental condition was performed four times. Our proteomics data is a compilation of only fully characterized proteins, with full gene ontology and function. Quantitative MS data, for each of the eight hormone stimulation conditions, was used to create a protein interaction map. The protein interaction network map, allows for a visual analysis of the Irisflorentin relationship of the interaction of each protein with the mutant AR. It is most likely that not all Dauricine proteins interact directly with the mutant AR, but can through intermediate proteins.