Proteolysis targeting chimeras (PROTACs) have emerged as a technology that can efficiently degrade target proteins. PROTACs are bifunctional molecules that hijack the ubiquitin proteasome system (UPS) to achieve degradation of proteins of interest (POIs) such as disease-related target proteins. Significantly the selective degradation of a broad spectrum of protein targets from transcription factors to enzymes has been reported. PROTACs consist of a ligand that binds to an E3 ligase, connected by an appropriately designed linker to a second ligand that binds to particular POIs. We recently reported the development of the first metallo-PROTAC, specifically a Pt-PROTAC, that can effectively degrade select Pt(II)-binding proteins. This novel Pt-PROTAC consists of an E3 ligase ligand connected by a linker to a Pt(II) centre via a stable amine carrier ligand and where the Pt(II) centre acts as a protein targeting warhead. Protein binding by this Pt-PROTAC will therefore instigate the formation of a ternary complex, PtBindingProtein-PtPROTAC-E3 ligase, and recruit E3 ligases to the vicinity of the PtBindingProtein, promoting ubiquitination and subsequent degradation by the proteasome through proteolysis. Our Pt-PROTAC prototype successfully degraded thioredoxin-1 and thioredoxin reductase-1 in multiple myeloma cancer cell lines.1 Furthermore the design and synthesis of a novel series of Pt-PROTACs will be described together with data concerning protein degradation activity and cell death analysis. Metallo-PROTACs may have important applications in the identification of metal binding proteins and as chemotherapeutic agents.