Affinity & 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.
Boost your research and commercialization goals by combining BLI and SPR at an attractive promotional price.
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.
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.
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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.
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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.
This application note discusses and characterizes of the interaction between the SARS-CoV-2 Nucleocapsid (N) protein and human chemokines.
A comprehensive guide for designing and performing assays that accurately measure the binding kinetics of biomolecular interactions and analyte concen...
Improve the overall drug discovery process to increase the success rate of preclinical candidates
Whether you're assessing FcRn-Antibody or FcγR-IgG binding interactions, you need a high throughput, versatile, and easy to use solution.
Assay design recommendations and best practices for producing the highest quality of kinetic data.
Antibody and other protein therapeutics are a major focus in drug discovery pipelines today
By Octet® Bio-Layer Interferometry (BLI) Platforms
For Accurate Determination of Kinetics and Affinity Rate Constants
Generate high-quality kinetics and affinity data in a fraction of the time compared to standard multi-cycle kinetics using the Octet® SF3.
Monitors up to 96 biosensors simultaneously, enabling label-free detection for protein quantitation and kinetic characterization at unmatched speed
Ideal for high-throughput applications that demand high sensitivity and low sample volume requirements
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