The complexity of polymer-protein interactions makes rational design of the best polymer architecture for any given biointerface extremely challenging, and the high throughput synthesis and screening of polymers has emerged as an attractive alternative. Here, we have adapted a porphyrin catalysed photoinduced electron/energy transfer - reversible addition-fragmentation chain transfer (PET-RAFT) polymerisation to enable high throughput synthesis of complex polymer architectures in dimethyl sulfoxide (DMSO) on low volume well plates in the presence of air. The polymerisation system shows remarkable oxygen tolerance, and excellent control of functional 3- and 4-arm star polymers. We then apply this methodology to investigate the effect of polymer structure on protein binding, in this case to the lectin concanavalin A (ConA). Recently, we have incorporated this technology into a highly automated liquid handling platform that allows us to reliably produce large libraries of diverse polymers in a high throughput manner. With this simple yet powerful technique, we are now discovering very well-defined polymer architectures capable of protein-like features. We anticipate that such an approach could be applied to screen the structure – activity relationships for any number of polymer-protein interactions.

Automated engineering of well-defined and protein-like biofunctional polymers

2019 Spring National Meeting

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