Kinetic & Affinity Characterization

  • Characterize the binding characteristics of your biologics molecules in real time
  • Accurately determine association and dissociation rate constants for your biomolecular interactions studies

Fc-gamma Receptor

Overview for Kinetic & Affinity Characterization

The establishment of the rate of interactions between two or more molecules and their rate of dissociation is key to understanding biological molecules complex formation and stability; two factors that are important in elucidating ligand-receptor binding mechanisms and stability during the development of biologics drug molecules. Two systems with the same affinity may 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. While ELISA has been the dominant technique in affinity characterization of biomolecules, real-time label free technologies have become increasingly popular due to their ability to provide more detailed information in the kinetics of binding of biomolecules.

  • Characterization of high affinity biologic interactions

    Characterization of high affinity biologic interactions

    Target binding characterization is an essential analytical step for the selection of high affinity (KD <1 nM) and highly specific biologics regardless of the types of molecules. A kinetic analysis further describes the components of association and dissociation that comprise the overall affinity interaction. For example, two lead compounds may possess a similar affinity (KD) to its target, but their differences in kinetic rate constants of association and dissociation can be used to estimate which will be more useful in vivo. Accurate analysis of these kinetic rate constants is therefore important information for lead selection and predicting the efficacy of protein therapeutics. The Pioneer SPR system with next generation SPR injections improves the efficiency of the characterization process over traditional SPR 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.

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    Fc receptor binding assays on the Octet system

    Fc Receptor Binding Assays on the Octet system

    The safety and efficacy of a therapeutic monoclonal antibody can be greatly impacted by its ability to bind to both the target and to the FcγR. Antibodies are often selected based on their binding properties to FcγRs. They are sometimes engineered to achieve desired FcγRs binding properties. As a result, the assessment of binding affinities of these antibodies to FcγRs is an integral part of biotherapeutic development processes.

    • 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

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  • Large molecules kinetics characterization

    Kinetics and Affinity Characterization

    The BLI Octet® family of instruments accurately measures 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.

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    Protein - Small molecules and peptide kinetics & affinity characterization

    Protein - Small molecules and peptide kinetics & affinity characterization

    Small molecule and peptide therapeutic drugs are highly sought after in most areas of disease research due to their desirable pharmacological properties and low propensity for immunogenicity. In small molecule drug discovery, the path to lead molecules can stem from many sources or starting points including fragment screening, high throughput screening, de novo structural design, etc. 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 ForteBio BLI Octet RED96e, Octet RED384 , HTX and Pioneer SPR platforms can be used to characterize small molecule and peptide systems.

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Resources for Kinetic & Affinity Characterization

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