A surface plasmon resonance spectroscopy method for characterizing small-molecule binding to nerve growth factor

5Citations
Citations of this article
9Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

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.

Cite

CITATION STYLE

APA

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

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free