Carna has developed a robust screening engine that make it possible to identify new generation of kinase inhibitor drugs to treat patients afflicted with serious diseases.
Carnaʼs powerful kinase drug discovery engine drives our pipeline expansion and the establishment of high-value partnerships. Our drug discovery programs begin with screening our vast lead-like compound library, followed by kinase profiling to select lead candidates, then optimization chemistry to identify highly selective drug candidates. We have established a collection of libraries consisting of kinase-focused and diverse-set compounds in order to maximize the success rate of screening. Carnaʼs CaRSKi, COPKi, CALKi, and CaPBA technologies, in combination with strategic synthetic and medicinal chemistry, uniquely position us to effectively design highly selective and effective inhibitors of kinase targets.
Technology Platform
CaRSKi Carna Rapid identification of
Selective Kinase inhibitors
High-throughput screening targeting single kinase with high quality kinase assay system followed by comprehensive kinase profiling to identify a highly selective lead compound.
COPKi Carna’s identification of Optimum
Profile Kinase inhibitors
Annotating compound library by kinome-wide screening against selected kinase panel followed by comprehensive kinase profiling to generate kinase fingerprints.
CALKi Carna’s identification of
ALlosteric Kinase inhibitors
As the cellular concentrations of ATP are high, typically 1‒5 mM, non-ATP competitive inhibitors would be more favorable for in vivo efficacy.
In addition to in vivo efficacy, generally non-ATP competitive inhibitors show excellent kinase selectivity as ATP pockets are highly conserved among kinases.
Carnaʼs MSA platform enables to screen compounds at both low and high ATP concentration.
CaPBA Carna Kinase Probe for
Binding Assay
High-throughput screening system targeting an unactivated conformation of a kinase using original probes, we can identify a potential inactive form binder which can interact with a latent pocket formed only in the inactive state of kinase.