The ability to imitate life formation processes holds exciting potential for understanding and controlling biological functions and addressing questions about the origins of life. Creating a fully artificial cell remains a significant challenge; however, researchers have made substantial progress in emulating various aspects of living systems, such as cell-like structures, growth and replication, communication, responsiveness, protein expression, and enzymatic activity. Moreover, artificial compartments have been previously used for TX-TL studies. Biomimetic compartment structures are essential components of artificial cells and include polymersomes, liposomes, coacervates, colloidosomes, virus-like particles, and protein cages. In particular polymersomes have attracted a lot of attention because they have significant advantages over non-polymerbased self-assemblies, including higher stability. Moreover, the chemical versatility of polymers can be leveraged to design polymersomes with multiple molecular functionalities such as degradability, stability, permeability and stimulus-responsiveness. Most bottom-up approaches to synthesize polymersomes have limitations due to the complexity of the preparation methodology or because of the low encapsulation efficiency of functional cargo. To address these limitations, researchers have turned to polymerization-induced self-assembly (PISA) as an effective method to produce polymer-based biomimetic structures, including polymersomes. PISA involves synthesizing amphiphilic block copolymers in aqueous solution by polymerizing a water-soluble monomer into a water-insoluble polymer block, using a hydrophilic polymeric initiator or chain transfer agent (CTA) for the hydrophilic block. During the initial phase of polymerization, the forming amphiphilic block copolymer is still soluble in water. Once the hydrophobic block has reached a certain length, the copolymers selfassemble. The hydrophobic block continues to grow in length so that the hydrophilic-to-hydrophobic ratio of the block copolymer decreases, and as a result, the morphology of the self-assembled structures evolves from micelles, over worm-like micelles, into vesicles. PISA is usually conducted with reversible-deactivation radical polymerizations (RDRPs), most prominently with reversible addition-fragmentation chain-transfer (RAFT) polymerisations, but also with atom transfer radical polymerizations (ATRP). PISA works under concentrated reagents conditions, resulting in high concentrations of self-assembled objects, and it allows highly efficient encapsulation of cargo in aqueous solutions in a one-pot procedure. Recently, PISA has been employed in the synthesis of biomimetic structures such as giant vesicles (GUVs) and polymersome nanoreactors, demonstrating the potential of this technique in the pursuit of artificial cells. Incorporating biological molecules in artificial cells requires biocompatible conditions, with PISA holding an advantage as it occurs in aqueous solutions. However, initiation conditions can potentially harm sensitive biological molecules. For instance, the high temperatures required for thermal initiators are not ideal when working with biomolecules. Light-triggered polymerisations are safer, especially when visible light is used, but biologically derived initiation may be ideal. An elegant approach would be to use biocatalytic initiation of RDRP systems. Recently, an enzyme-initiated PISA was reported by Tan and coworkers, which employed horse radish peroxidase (HRP) to initiate RAFT polymerisation. However, this approach necessitates hydrogen peroxide and the formation of free radicals to initiate the reaction, which could lead to cytoxicity. Moreover, the use of biologically relevant buffers as solvent led to unstable nanoparticles and as such deionised water was employed. Therefore, a more robust bioPISA technique is needed to couple the synthesis and self-assembly of polymers through PISA with biological or bio-mimetic systems. Biocatalytic ATRP (bioATRP) uses enzymes or their cofactors to initiate and control radical polymerisations and was introduced simultaneously by our group and di Lena and co-workers. A wide range of biologically derived catalysts have been employed as ATRPase, such as horseradish peroxidase, 44 laccase, 46 catalase, 47 haemoglobin (Hb), . This paves the way for a biocatalytic PISA methodology based on enzyme-mediated ATRP (Figure ).