The invention relates to the preparation of bi-functional compounds I [ARB is an AR binding moiety that does not bind to a ligand binding domain; E3LB is an E3 ligase binding moiety; L is a linker coupling the AR binding moiety to the E3 ligase binding moiety], which function to recruit endogenous proteins to an E3 ubiquitin ligase for degradation, and methods for using same. More specifically, the invention provides specific proteolysis targeting chimera (PROTAC) mols. which find utility as modulators of targeted ubiquitination of a variety of polypeptides and other proteins, in particular the androgen receptor of a slice variant of AR which lacks the ligand binding domain, labeled as AR-V7, which are then degraded and/or otherwise inhibited by the compounds as described herein. Thus, II was prepared starting from (S)-1-(4-bromophenyl)ethylamine by a multistep procedure (procedure given). II decreased the cell count of human prostate cancer 22RRv1 in a concentration-dependent manner. Immunoblots demonstrated that II‘s degradation concentration 50% (DC₅₀) for AR-V7 and AR-FL was 0.37 and 2μmol/L, resp., demonstrating that II was able to degrade both AR-V7 and AR-FL, although the degradation effect was more efficient against AR-V7 compared to AR-FL. To assess the potential therapeutic role of II, 12 human prostate cancer cell lines were generated that are resistant to the four FDA-approved SAT agents-abiraterone, enzalutamide, apalutamide, and darolutamide. When resistant cells were treated with II, decreased cellular proliferation and reduced tumor mass were observed both in vitro and in mice. II inhibited prostate cancer cellular proliferation and increased apoptosis only in androgen-responsive prostate cancer cells.