Small-molecule inhibitors have been previously investigated to identify possible therapeutics for the treatment of chronic pain. In the present study, known nerve growth factor (NGF) inhibitors identified by 125I-NGF binding were characterized using affinity and binding evaluations by surface plasmon resonance (SPR) spectroscopy. A novel strategy for characterizing NGF inhibitors was used to determine the binding affinity (KD) and saturation ability of each compound with immobilized NGF. Seventy-four percent of compounds screened demonstrated a positive binding event to NGF. A KD less than 10 μM and a percent saturation greater than 50% were used as thresholds to identify inhibitors that would warrant further investigation. This study details for the first time a methodology that can be used to directly characterize the binding event between small-molecule inhibitors and NGF.
CITATION STYLE
Kennedy, A. E., Sheffield, K. S., Eibl, J. K., Murphy, M. B., Vohra, R., Scott, J. A., & Ross, G. M. (2016). A surface plasmon resonance spectroscopy method for characterizing small-molecule binding to nerve growth factor. Journal of Biomolecular Screening, 21(1), 96–100. https://doi.org/10.1177/1087057115607814
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