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European Biopharmaceutical Review

Investigating Interactions

 

As a result of scientific efforts over the last few decades, the Protein Data Bank (PDB) library now contains descriptions of more than 48,000 high-resolution biomolecular structures (1). In addition, characterisation data for more than 38,000 of the estimated 300,000 protein-protein interactions in humans has been collected (2). This information is critical to our understanding of interactions between proteins and in the investigation of the effects of these interactions, from academic research to drug discovery and development. Based on the report by Prasad et al, it can be calculated that only around six per cent of the identified interactions have been confirmed in vivo and with the use of several in vitro techniques (2). Thus, although a significant number of interactions are already well-characterised, there is still a need for additional experimental verification.

As well as the need for investigation of protein structure-function relationships and the mapping of the interactome to increase our biological understanding, there is also a growing demand from regulatory authorities to employ orthogonal approaches to biotherapeutic discovery and development. Complementary methods are needed to enable researchers to validate and verify interaction data, and to make confident conclusions and decisions in the drug development process.


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Thomas Lundbäck is a Senior Project Manager at GE Healthcare, Life Sciences. He recently joined GE Healthcare from Biovitrum, where he held the positions of project leader and principal scientist, implementing different biophysical techniques. Thomas has a PhD in biophysical chemistry from the Karolinska Institute in Stockholm, Sweden. He is also a member of the Industrial Research Committee at the Royal Swedish Academy of Engineering Sciences (IVA), which represents research areas of future strategic interest for Swedish industry.
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