Protein Interaction Testings
Biotherapeutic Drug Discovery With SPR
Lead Characterization Of High Affinity Biologic Interactions With SPR

Lead Characterization Of High Affinity Biologic Interactions With SPR

At Seattle Genova, we are providing the most comprehensive lead characterization of high affinity biologic interactions with SPR. Protein therapeutics, or biologics, are known for having good specificity for their therapeutic targets and this often affords fewer side effects than small molecule drugs. Biologics are a viable route for targeting protein–protein interactions, cell surface receptors, and other difficult-to-drug therapeutic targets.

Primary screening techniques for biologics normally focus on speed and throughput to identify hits from libraries containing 104–105 crude protein samples. Secondary and tertiary screens can be used to further test the hits for functional binding effects or cross-reactivity. Once a panel of advanced hits has been compiled, they can be expressed and purified in small scale for in depth characterization before in vivo testing.

Target binding characterization is an important analytical step for the selection of high affinity (KD<1nM) and highly specific biologics regardless of the types of molecules. Kinetic analysis further describes the components of association and dissociation that comprise the overall affinity interaction.


As new hits are generated and optimized into lead candidates, we can accurately characterize target binding for panels of advanced hits all the way to high affinity leads.

• Our service is 3- to 6-fold faster than traditional characterization services

• We use less sample (50% less analyte)

• No analyte dilutions required

Baseline stability coupled with the time and injection reducing advantages make our service an optimal assay platform for high affinity biologic characterization. 


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