Key Highlights

  • Easily measure direct compound binding down to at least 500 Da

  • High-capacity array allows for analysis of a broad panel of targets and off-targets

  • Both weak- and high-affinity interactions are readily quantitated


While phosphorylation plays a critical role in the regulation of many biological processes, when unchecked it can result in cell hypertrophy and contribute to the development of cancer. Hyperactivity of protein kinases is a key driver for unrestricted phosphorylation. Protein kinases as a drug target class present challenges owing to the widespread involvement of phosphorylation across pathways and the sharing of conserved regions among many kinases. As a result, effective targeting of protein kinases must include a strategy to minimize off-target effects.

Following on this, we describe here an approach to screening kinase inhibitors by HT-SPR on the LSAXT platform. Using the LSAXT, both quantitative kinetics and selectivity can be determined for up to hundreds of targets and off-targets in parallel. The array format of HT-SPR makes it very practical to screen these hundreds of interactions simultaneously and minimize time and reagent consumption. In addition, the increased sensitivity of the LSAXT enables confident measure for this class of molecules. While protein kinases are used here as an example, any therapeutic strategy focused on understanding and minimizing off-target effects can benefit from this approach.

Posted by Rebecca Rich

To download the rest of the application note, please fill out the short form below. Thank you.