A surface plasmon resonance facility for label-free analysis of biomolecular interactions

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Life at the molecular level relies on a multitude of intimate, reversible interactions. In the case of macromolecules like proteins, these interactions are responsible for the formation of large multi-subunit complexes, like those that stabilise machineries required to synthesise our genetic material (DNA and RNA polymerases) and all proteins in our body (ribosomes). Other contacts are necessary to stabilise structures that are visible to the naked eye, like the keratin in our hair and nails or the collagen fibres that serve as a flexible scaffold to support different tissues. Some of these interactions are transient, lasting less than a second, whereas others have much longer lifetimes. Determining the strength and the speed of these interactions is essential to identify their biological relevance, e.g. to learn how cells assemble our bodies, generate energy and combat different types of infections. This information is also the basis of important agricultural, biotechnological, medical and industrial applications. For example, modern agrochemical and drug design involves development of a specific ligand (acting as a 'key') that modulates a protein in our cells (acting as a 'lock'). Starting with a poorly binding 'key', cycles of modification with new chemical entities and binding analyses are required to obtain improved versions that recognise a desired 'lock' - leading to compounds that we eventually see as drugs in the market. Surface plasmon resonance (SPR) is currently the gold-standard technique to accurately measure these interactions. Our aim is to replace obsolete equipment at Imperial College London with the latest SPR equipment to allow researchers to accelerate their investigations with this technology.