Label Free Affinity & Kinetic Characterization
Establishing the kinetics for binding between two or more biological or small molecules is key to understanding molecular complex formation and can help in elucidating ligand-receptor binding mechanisms and stability during the development of biologics drug molecules. Two systems with the same affinity could exhibit completely different binding mechanisms. Hence, the evaluation of the affinity constants in conjunction with the association and dissociation rates of binding is crucial in the selection process for optimal drug candidates. Octet assays have become increasingly popular for affinity characterization of biomolecules due to their ability to provide more detailed information in the kinetics of binding of biomolecules.
Large Molecules Kinetics Characterization
The Octet family of instruments accurately measure kinetic constants by bringing the detection surface directly to the sample, eliminating the need for microfluidics. This unique approach utilizing label-free, real-time analysis streamlines laboratory workflow and expedites assay development. It allows direct measurement of crude samples while minimizing instrument maintenance. It is extremely versatile in large molecules kinetics characterization and enables rapid assay optimization to allow for the analysis of molecules ranging from recombinant proteins and antibodies to viruses and nanoparticles.
Fc Receptor Binding Assays on the Octet System
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 safety and efficacy can be greatly impacted by their binding to both the target and to FcγRs.
- Octet systems offer high throughput and sensitive methods for Fc receptor binding analysis
- A variety of biosensor surfaces are available and allow for flexibility and rapid optimization of assay format
Protein - Small Molecules 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 amongst others. The determination and evaluation of 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 process are essential to accurately determine biological potency in vitro so that structure-activity relationships (SAR) can be used for efficient structural design. Learn how Octet RED96e, Octet RED384, Octet HTX and Pioneer SPR platforms can be used to characterize small molecule and peptide-protein binding.
High Affinity Interactions
Target binding characterization is an essential analytical step for the selection of high affinity and highly specific biologics regardless of the types of molecules. The characterization of biological molecules with relatively high affinity for each other (KD <1 nM) is however often quite challenging due in part to the need for high sensitivity analytical platforms that are capable of detecting slight changes in responses. The Pioneer SPR is a high sensitivity instrument that utilizes next generation SPR injections to improve the efficiency of the characterization process by determining the kinetics and affinity in a single step. The next-generation OneStep gradient injection featured on the Pioneer platform dramatically increases the speed of affinity characterization while maintaining accuracy and high confidence in results.