Label-Free Affinity and Kinetic Characterization
Establishing an in-depth understanding of binding interactions between biological or small molecules is vital to elucidating ligand receptor binding mechanisms and stability during the development of drug molecules. Drugs that exhibit similar affinities could exhibit diverse binding mechanisms and kinetics. Hence, the evaluation of affinity constants in conjunction with association and dissociation rates provides crucial information for lead selection. Octet® BLI assays have become increasingly valuable for affinity and kinetic characterization of biomolecules.
Featured Applications
Large Molecules Kinetics Characterization
The Octet® BLI platform accurately measures kinetic constants by bringing the detection surface directly to the sample, eliminating the need for microfluidics. This unique approach using label-free, real-time analysis streamlines laboratory workflows and expedites assay development. The unique platform allows direct measurement from crude samples while minimizing instrument maintenance. It is extremely versatile in large molecules kinetics characterization and enables rapid assay optimization to allow the analysis of molecules ranging from recombinant proteins and antibodies to viruses and nanoparticles.
Fc Receptor Binding Assays on the Octet® BLI Platform
The selection of desired antibody-based therapeutics is often based on binding properties, including binding to FcγRs. Antibodies are sometimes engineered to achieve desired FcγRs binding properties, as their binding can greatly impact 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 for accurate determination of biological potency in vitro so structure-activity relationships (SARs) can be used for efficient structural design. Learn how the 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-affinity Interactions
Target binding characterization is an essential analytical step for selecting high-affinity and specific biologics, regardless of molecule type. The characterization of biological molecules with relatively high-affinity target binding (KD <1 nM) is often quite challenging due to the need for high-sensitivity analytical platforms capable of detecting slight changes in responses. The Octet® SF3 instrument is a high-sensitivity instrument that utilizes next generation SPR injections to improve the efficiency of the characterization process by determining kinetics and affinity in a single step. The OneStep® and NeXtStep™ Gradient Injection technologies featured on the Octet® SF3 instrument dramatically increases the speed of affinity characterization while maintaining accuracy and high confidence in results.
Featured Resources
Instant Access
Kinetic Analysis of Antibody Binding to an Expressed Membrane Protein on Captured Lipoparticles
PDF | 929.6 KB
Fragment-Based Drug Discovery (FBDD) Using Octet® SPR OneStep® and NeXtStep™ Injections
PDF | 5.1 MB
