Affinity assays for decrypting protein targets of unknown function

Matthew J Todd; Maxwell D Cummings; Marina I Nelen

doi:10.1016/j.ddtec.2005.08.015

Affinity assays for decrypting protein targets of unknown function

Drug Discov Today Technol. 2005 Autumn;2(3):267-73. doi: 10.1016/j.ddtec.2005.08.015.

Authors

Matthew J Todd¹, Maxwell D Cummings², Marina I Nelen²

Affiliations

¹ Johnson & Johnson Pharmaceutical Research & Development, L.L.C., 665 Stockton Drive, Exton, PA 19341, USA. Electronic address:mtodd3@prdus.jnj.com.
² Johnson & Johnson Pharmaceutical Research & Development, L.L.C., 665 Stockton Drive, Exton, PA 19341, USA.

PMID: 24981946
DOI: 10.1016/j.ddtec.2005.08.015

Abstract

The application of label-independent biophysical assays (affinity assays) to carefully selected libraries of biochemicals, natural products and known bioactive molecules generates a powerful tool to identify ligands indicative of protein function. Detection of ligand binding does not require the measurement of enzyme activity, thus every cofactor, ion, reactant or product might be identified separately. One such assay, ThermoFluor(®), monitors ligand perturbation of protein thermostability. In conjunction with a functional probe library (FPL), this assay has been used to decrypt the function of orphan proteins.: