Biologics and Small Molecules Research
- Measure target binding affinity and kinetics of purified and non-purified biological molecules
Rapidly perform DOEs to screen optimal assay conditions
The development of biologics-based drugs is an expensive and lengthy process. During early discovery, researchers must select multiple lead candidates, confirm mechanisms of action (MOA) against the target and investigate optimal conditions for production and functional activity before looking into their downstream critical quality attributes (CQAs). The Octet® system provides unmatched ease-of-use and throughput capability in research and assay development for screening and characterization purposes.
Fc Receptor Binding Assays on the Octet® BLI Platform
The selection of desired antibody-based therapeutics is often based on their binding properties, including binding to FcγRs. Antibodies are sometimes engineered to achieve desired FcγRs binding properties, as their binding can greatly impact their safety and efficacy to both the target and to FcγRs.
- Octet® BLI systems offer a high throughput, sensitive solution for Fc receptor binding analysis
- A variety of assay-ready biosensor surfaces are available and allow for flexibility and rapid optimization of assays
Small Molecule and Peptide Binding Kinetics
The discovery of small molecule and peptide lead molecules can stem from many sources, including fragment screening, high throughput screening and de novo structural design. Determining and evaluating the affinity of small molecule binding to a therapeutic target is a significant component of the drug discovery process and lead optimization. The hit-to-lead and lead optimization processes are essential to accurately determine biological potency in vitro so structure-activity relationships (SARs) can be used for efficient structural design. Learn how Octet® R series as well as Octet® RH16, Octet® RH96 and Octet® SF3 instruments can be used to characterize small molecule and peptide binding.
High Throughput Phage Display Screening
Phage display is a technique for enabling the study of protein, peptide or DNA interactions with a target protein. This technology enables discovery of high-affinity binders by using bacteriophages to present a target protein on the exterior of the viral coat (while containing the DNA encoding the target protein inside the viral coat). Resulting phages can be screened for binding against a library of peptides or proteins in a high throughput fashion.
Due to its high throughput design, the Octet® BLI system is routinely used as a secondary screening platform for Fab fragments and non-antibody ligands derived from phage display libraries. Such a screen can provide affinity ranking data and estimates of association and dissociation constants for primary hits.
Characterize Irreversible Inhibitors and Measure Commitment to Covalency
The majority of small molecule inhibitor assays tested with label-free, real-time biosensor technologies are reversible interactions, characterized by commonly used kinetic rate models. However, a significant fraction of therapeutic enzyme inhibitors on the market function through covalent modification of the target.
The Octet® SF3 system is a SPR platform that can be used with regenerable Streptavidin biosensors to reversibly capture protein targets and quantify the efficiency of covalent inhibitors binding to the target. The irreversible inhibitor applications method can be used to determine inhibitor compound's commitment to covalency (Cc) as a metric for irreversible inhibitors.