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Biomolecular interactions are the measure of binding mechanisms and parameters between various forms of biomolecules, useful for obtaining crucial binding data that give insight into protein functions, aid in antibody or assay development, and for evaluating candidates in drug discovery.
We provide high-throughput kinetics and affinity characterization using Nicoya Lifesciences SPR, and gold-standard binding affinity, thermodynamic, and stoichiometry data on the Malvern Microcal PEAQ-ITC.
Proteins, Lipids, Carbohydrates, Antibodies, Nucleic acids, Small molecules, Cells, Viruses, Nanoparticles, Virus-like particles, Crude Samples (serum, supernatants etc)
Contact us to discuss your analytical needs
Biomolecular interactions govern the everyday functions of the body and are typically measured using ligand-binding assays. An interaction system can be protein-ligand, protein-protein, protein-nucleic acid, but can also be more complex systems such as virus-like particles and antibody-drug conjugates.
Current label-free techniques are able to generate high-quality steady-state affinity and kinetics data that goes beyond yes-or-no answers from co-immunoprecipitation or the less-accurate ELISA studies.
In the era of rapidly evolving biologics, ligand-binding assays have gained importance in every step of drug discovery, drug development, pharmacokinetic analysis, safety, and immunogenicity evaluation, and biomarkers discovery processes. High-quality ligand-binding assay data on affinity and kinetics are an requirement for New Drug applications (NDAs).