Developing and investigating an ultra-stable molecular hub for bionanotechnology

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When biologists wish to isolate or immobilise an object (proteins, DNA, RNA, sugars, small organic molecules, nanoparticles), they will very often attach the vitamin biotin to this object, so that the object can be captured by the protein streptavidin. The link from biotin to streptavidin is one of the strongest known in nature, but this link can be broken in challenging situations, so limiting many biological experiments and devices. We have made an altered streptavidin which forms an even stronger link to biotin, so that biotin is captured for longer and stays bound in harsher conditions. We plan to determine at the atomic level why this new interaction is stronger. This insight should help to illuminate the basis of ultra-strong binding, and so assist the design of drugs that can bind more stably to their targets and thus be more effective. We will also engineer streptavidin so that it can anchor two different kinds of molecules, enabling biologists to create new assemblies to combine and control the functions of biomolecules. We ourselves will use these assemblies to explore how growth factors can either work together or compete in transmitting signals inside the cell, so determining whether the cell lives, dies, or divides.