Antibody-Inspired Affinity Measurements of Fluorescein-Linked Small Molecule Ligands

29 May 2020, Version 1
This content is a preprint and has not undergone peer review at the time of posting.

Abstract

The availability of reliable methods for the characterization of the binding of small molecule ligands to protein targets is crucially important for Drug Discovery. We have adapted a method, routinely used for the characterization of monoclonal antibodies (Enzyme-linked immunosorbent assay, or “ELISA”), to small molecule ligands, using fluorescein conjugates and anti-fluorescein antibodies as detection reagents. The new small molecule-ELISA methodology was tested using a panel of binders specific to carbonic anhydrase II, with dissociation constants ranging between 6 uM and 14 nM. An excellent agreement was found between ELISA measurements and fluorescence polarization results. The methodology was also extended to BIAcore measurements and implemented for ligands coupled to oligonucleotides. Small molecule-ELISA procedures are particularly useful in the context of DNA-encoded libraries, for which hit validation procedures need to be performed on dozens of candidate molecules and hit compounds can be conveniently resynthesized on DNA.

Keywords

Affinity Measurement
ELISA technique
surface plasmon resonance binding affinity experiments
Binding assays
DNA-Encoded Library

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