Sapidyne Instruments

Selected KinExA References

Affinity & Kinetic Measurements:

KinExA technology overview:

KinExA’s role in drug discovery:

  • Erasmus MF, Dovner M, Ferrara F, D’Angelo S, Teixeira AA, Leal-Lopes C, Spector L, Hopkins E, Bradbury ARM. Determining the affinities of high-affinity antibodies using KinExA and surface plasmon resonance. MAbs. 2023 Jan-Dec;15(1):2291209. doi: 10.1080/19420862.2023.2291209. Epub 2023 Dec 13. PMID: 38088807; PMCID: PMC10793667
  • Darwish IA. Kinetic exclusion assay technology: Theory, experimental aspects, and applications in concentration measurements across diverse fields. Profiles Drug Subst Excip Relat Methodol. 2026;51:351-415. doi: 10.1016/bs.podrm.2025.12.005. Epub 2026 Jan 8. PMID: 41714070
  • Danial M, et al. 2017. Site-Specific Polymer Attachment to HR2 Peptide Fusion Inhibitors against HIV-1 Decreases Binding Association Rates and Dissociation Rates Rather Than Binding Affinity. Bioconjug Chem. 10.1021/acs.bioconjchem.6b00540.
  • Kariolis MS, et al. 2017. Inhibition of the GAS6/AXL pathway augments the efficacy of chemotherapies. J Clin Invest. 10.1172/JCI85610.
  • Fan Y., et al. 2016. Immunological Characterization and Neutralizing Ability of Monoclonal Antibodies Directed Against Botulinum Neurotoxin Type H. The Journal of Infectious Diseases 15;213(10):1606-14.
  • Köck, K., et al. 2015. Preclinical development of AMG 139, a human antibody specifically targeting IL-23. British Journal of Pharmacology 172:159-172.
  • Tabrizi M.A., et al. 2009. Translational strategies for development of monoclonal antibodies from discovery to the clinic. Drug Discov Today 14(5/6): 298-305.

Significance of “solution phase” measurements to unmodified molecules:

Comparison to SPR:

Sensitivity to measure tight binders:

Reverse assay techniques:

Whole cell binding techniques:

  • Chen, P., Bordeau, B.M., Zhang, W. et al. Investigations of Influence of Antibody Binding Kinetics on Tumor Distribution and Anti-Tumor Efficacy. AAPS J 27, 91 (2025). https://doi.org/10.1208/s12248-025-01076-z
  • Grier, M.; McBride, H.J.; Glass, T.R.; Chen, Q. Kinetic Exclusion Assay Using Cellular Membranes for Affinity Determination of Anti-CD20 Antibody. In Resistance to Anti-CD20 Antibodies and Approaches for Their Reversal; Elsevier, 2024; pp. 249–269 ISBN 978-0-443-19200-5
  • Bedinger, D., et al. 2015. Differential pathway coupling of activated insulin receptor drives signaling selectivity by XmetA, an allosteric partial agonist antibody. J Pharmacol Exp Ther 353(1):35-43.
  • Rathanaswami P., Babcook J., Gallo M. 2008. High-affinity binding measurements of antibodies to cell-surface-expressed antigens. Anal Biochem 373: 52-60.
  • Xie L., et al. 2005. Measurement of the functional affinity constant of a monoclonal antibody for cell surface receptors using kinetic exclusion fluorescence immunoassay. J Immunol Methods 304: 1-14.

Unpurified antigens:

Other interesting studies:

  • Li X., Kaattari S.L., Vogelbein M.A., Vadas G.G., Unger M.A., 2016. A highly sensitive monoclonal antibody based biosensor for quantifying 3-5 ring polycyclic aromatic hydrocarbons (PAHs) in aqueous environmental samples. Sens Biosensing Res. 7:115-120.
  • Lou J., et al. 2010. Affinity maturation of human botulinum neurotoxin antibodies by light chain shuffling via yeast mating. Protein Eng Des Sel 23(4): 311-319.
  • Kahle K.M., Steger H.K., Root M.J. 2009. Asymmetric deactivation of HIV-1 gp41 following fusion inhibitor binding. PLOS Path 5(11): 1-11.
  • Nowakowski A., et al. 2002. Potent neutralization of botulinum neurotoxin by recombinant oligoclonal antibody. Proc Natl Acad Sci 99: 11346-11350.

Immunoassay Techniques:

  • Darwish, I.A.; Wang, Z.; Darling, R.J. Development and Comparative Evaluation of Two Highly Sensitive Immunosensor Platforms for Trace Determination of Copper Ions in Drinking Water Using a Monoclonal Antibody Specific to Copper-EDTA Complex. Molecules 2023, 28, 7017, doi:10.3390/molecules28207017
  • Darwish I.A., et al. 2013. Kinetic-exclusion analysis-based immunosensors versus enzyme-linked immunosorbent assays for measurement of cancer markers in biological specimens. Talanta 111: 13-19.
  • Prieto-Simon B., Miyachi H., Karube I., Saiki H. 2010. High-sensitive flow-based kinetic exclusion assay for okadaic acid assessment in shellfish samples. Biosens Bioelectron 25: 1395-1401.
  • Sasaki K., Oguma S., Namiki Y., Ohmura N. 2009. Monoclonal antibody to trivalent chromium chelate complex and its application to measurement of the total chromium concentration. Anal Chem 81: 4005-4009.
  • Glass T.R., Ohmura N., Saiki H. 2007. Least detectable concentration and dynamic range of three immunoassay systems using the same antibody. Anal Chem 79: 1954-1960.
  • Bromage E.S., et al. 2007. The development of a real-time biosensor for the detection of trace levels of trinitrotoluene (TNT) in aquatic environments. Biosens Bioelectron 22: 2532-2538.
  • Sasaki K., Glass T.R., Ohmura N. 2005. Validation of accuracy of enzyme-linked immunosorbent assay in hybridoma screening and proposal of an improved screening method. Anal Chem 77: 1933-1939.
  • Glass T.R., et al. 2004. Use of excess solid-phase capacity in immunoassays: advantages for semicontinuous, near-real-time measurements and for analysis of matrix effects. Anal Chem 76: 767-772.
  • Ohmura N., Lackie S., Saiki H. 2001. An immunoassay for small analytes with theoretical detection limits. Anal Chem 73: 3392-3399.