Kinase Inhibitors
Expand selectivity profiling to include up to hundreds of targets and off-targets in replicate in a single experiment. Enable detailed kinetic analysis across weak and high affinity binders in parallel. Distinguish subtle differences in selectivity with a high degree of accuracy. Throughput avoids the need to keep fragile kinases active for days of screening.
- Selectivity: Comprehensively screen candidates against hundreds of targets and off-targets
- Resolution: Quantitatively determine subtle differences in association and dissociation kinetics
- Broad dynamic range: Accurately determine kinetics for both weak and high affinity interactions in the same experiment
Selectivity of sunitinib against panel of kinases in duplicate.
GSK-461364 binding to an array of kinases in duplicate. High selectivity is demonstrated for only PLK1 as expected.
Carterra is pleased to have collaborated with Carna Biosciences to develop kinase drug discovery. The data presented above was generated with kinases from Carna Biosciences. For more information about Carna Biosciences kinase products, click here.
Fragment Screening
Fragment-Based Lead Discovery (FBLD) has emerged as a core approach to early-stage hit finding in drug discovery programs. This form of drug discovery is distinguished by the screening of libraries of very small chemical compounds that bind with low-affinity to therapeutic targets. Screening small compounds allows for an efficient sampling of the chemical space relevant to medicinal chemistry.
Carterra Ultra® offers the enhanced speed and sensitivity necessary to support FBLD. Ultra’s large ligand array allows for many targets, off targets, mutants, and multiple species to be measured in parallel; a 100-fold enhancement over other SPR systems. You can utilize ready-made panels of biotinylated-proteins to standardize the assay parameters so you can move directly to finding hits and drive your medicinal chemistry programs.
Affinity determination for AMP-PNP against captured kinases. Triplicate dose-responses are overlayed. The last 5 seconds of data points from the association phases were averaged and plotted on the Y-axis against the log of the analyte concentration (X-axis) in the insets. Fits to these curves yielded the equilibrium KD values and standard errors as reported by Kinetics and shown for each panel.
Example data taken from the new screening tab in Kinetics 2.0. The binding levels of analyte replicates (purple) are shown vs. injection order for easy assessment of on-chip target stability. Hovering over individual data points will trigger a pop-up showing the injection cycle that generated the point allowing for fast sensorgram quality control and false-positive elimination. Structure view is added for clarity here and not present in the analysis software.