Surface plasmon resonance in biotechnical development

Molecular interactions, and more specifically biomolecular interactions, are studied and measured in order to predict behavior in living systems. In medical and pharmaceutical studies, the interaction of e.g. two proteins with each other is of importance to be able to predict the events in a human body. Many techniques to study protein-protein interactions exist, all with their own advantages and drawbacks. Surface plasmon resonance (SPR) has become one of the most widely applied techniques ever since the availability of the first commercial instruments in the 1990s. With this technology, protein-protein interactions are measured in real-time and essentially label-free [1,2]. Within the area of biotechnology SPR is commonly used both to assess potential therapeutics that bind certain target molecules and to develop new and specific purification and diagnostic tools. Due to the recently established protein selection strategies that open up the possibility of customized binders, this type of binders is increasing both in numbers and usability. Within this workshop we will discuss different strategies for development and characterization of binders for various purposes.

[1] de Mol, N. J. and Fischer, M. J. Surface plasmon resonance: a general introduction. Methods Mol.Biol. 2010; 627 1-14

[2] Willander, M. and Al-Hilli, S. Analysis of biomolecules using surface plasmons. Methods Mol.Biol. 2009; 544 201-229

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