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Living materials are based on proteins that adapt and change in structure and function continuously when in use; cellular microtubules, ATP synthases and ribosomes are but a few examples. Breathing life into semi-synthetic materials would allow improved understanding over protein regulation and dynamics, and how their integration into complex systems can lead to emergent functions across length scales. The focus of my research is to achieve optical control over functional proteins by connecting them to artificial molecular switches, with the aim to amplify molecular switching events across length scales and gain understanding over cooperative and systematic regulations of proteins. We choose light because it offers spatiotemporal selectivity, is compatible with a wide range of phases and relatively non-destructive towards protein systems. Interfering with mechanisms such as allosteric communication or hierarchical self-assembly not only paves the way towards an improved understanding of cooperative or collective effects in living matter, but it is also associated with the generation of new classes of smart bio-hybrids. The works presented in this thesis involve diverse functional proteins, ranging from an allosteric transport protein, the human serum albumin (Chapter 3), to proteins forming cages (Chapter 4, 5, 6) all the way to chaperone proteins that are known to assist cellular protein folding (Chapter 6). Overall, we have developed photo-responsive protein-based hybrids in which dynamic regulations such as allostery and self-assembly are prominent to protein functionality. Via incorporation of photo-switches, optical control has been demonstrated across length scales, from a monomeric structure to highly defined multimeric architectures made of proteins. The presented research provides a means to interfere with dynamic regulations of proteins and supports strategies towards the development of biocompatible and smart materials

Optical control over monomeric and multimeric protein hybrids