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home > ebr > winter 2003 > understanding drug-kinase interactions with surface plasmon resonance (spr)
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European Biopharmaceutical Review

Understanding Drug-Kinase Interactions with Surface Plasmon Resonance (SPR)

Protein kinases (PKs) represent one of the largest known superfamilies of human proteins. A recent report identified 510 candidate PK genes on the basis of sequence homology (1). PKs play critical roles in almost all signal transduction pathways, such as post-receptor cascades (2). Upstream signalling events are relayed by the action of PKs, usually via their phosphorylation of key serine, threonine or tyrosine residues on target proteins, using ATP or GTP as phosphate donors (3). These functions are carried out by a 250 amino acid catalytic domain, which is conserved among and used to identify members of the PK superfamily (4). This domain consists of an N-terminal lobe that binds and orientates the ATP/GTP, and a larger C-terminal lobe, which binds to the target protein and catalyses the transfer of phosphate.

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By Robert Karlsson, Director of Biochemistry and Chemistry at Biacore AB

Robert Karlsson joined Biacore in 1986 as one of the first five scientists in the company. In Biacore he has held several positions in both R&D and marketing. Mr Karlsson is currently Director of the Biochemistry and Chemistry Department of Biacore R&D at Biacore AB, with responsibility for leading both operational activities and the strategic development in these disciplines. Mr Karlsson has over 25 years' experience in the pharmaceutical and biotech industry. He has published around 30 papers on different aspects of Biacore analysis including methodology papers on mapping, kinetics, thermodynamics and concentration analysis, as well as application oriented papers on drug screening and ADME assays.

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Robert Karlsson
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