Drug development using protein-based therapeutics has become particularly important in medical research and is predicated on the identification of therapeutic targets. The drug development process is generally a long and costly process and only a very small percentage of drug candidates under development make it through to approval by the regulatory bodies.

Determination of accurate kinetics and affinity along with other critical quality attributes play an ever-increasing important role in identifying and isolating therapeutic molecules to drug-target. It is important therefore, that any systems developed for these purposes can match not only the high throughput needs of the user but also their sensitivity needs; allowing assays to be performed earlier in the workflow with minimal amounts of precious samples. This faster time to results allows assessment of accurate and precise data earlier in the workflow and as such quicker decisions can be made on which lead candidates to promote.

Kinetic analysis trastuzumab binding HER2 High affinity kinetic interactions are often poorly defined due to the lack of curvature in the association phase and may require in excess of an hour to approach equilibrium. Therefore, the resolving power of a single analyte injection must not be at the expense of resolution or throughput. Initial analysis of the trastuzumab HER2 kinetics and affinity determined by multi-cycle kinetics on the Octet^®SF3 are shown in Table 1 and the associated sensorgram shown in figure 1.