Integration of Affinity Selection-Mass Spectrometry and Functional Cell-Based Assays to Rapidly Triage Druggable Target Space within the NF-κB Pathway

J Biomol Screen. 2016 Jul;21(6):608-19. doi: 10.1177/1087057116637353. Epub 2016 Mar 11.

Abstract

The primary objective of early drug discovery is to associate druggable target space with a desired phenotype. The inability to efficiently associate these often leads to failure early in the drug discovery process. In this proof-of-concept study, the most tractable starting points for drug discovery within the NF-κB pathway model system were identified by integrating affinity selection-mass spectrometry (AS-MS) with functional cellular assays. The AS-MS platform Automated Ligand Identification System (ALIS) was used to rapidly screen 15 NF-κB proteins in parallel against large-compound libraries. ALIS identified 382 target-selective compounds binding to 14 of the 15 proteins. Without any chemical optimization, 22 of the 382 target-selective compounds exhibited a cellular phenotype consistent with the respective target associated in ALIS. Further studies on structurally related compounds distinguished two chemical series that exhibited a preliminary structure-activity relationship and confirmed target-driven cellular activity to NF-κB1/p105 and TRAF5, respectively. These two series represent new drug discovery opportunities for chemical optimization. The results described herein demonstrate the power of combining ALIS with cell functional assays in a high-throughput, target-based approach to determine the most tractable drug discovery opportunities within a pathway.

Keywords: ALIS; NF-κB pathway; NF-κB1/p105; TRAF5; affinity selection; high-throughput screening; mass spectrometry; phenotypic screening.

MeSH terms

  • Drug Discovery*
  • High-Throughput Screening Assays / methods*
  • Ligands
  • Mass Spectrometry / methods
  • NF-kappa B / antagonists & inhibitors*
  • NF-kappa B / chemistry
  • Protein Binding
  • Signal Transduction / drug effects
  • Structure-Activity Relationship*
  • TNF Receptor-Associated Factor 5 / antagonists & inhibitors
  • TNF Receptor-Associated Factor 5 / chemistry
  • Transcription Factor RelA / antagonists & inhibitors
  • Transcription Factor RelA / chemistry

Substances

  • Ligands
  • NF-kappa B
  • RELA protein, human
  • TNF Receptor-Associated Factor 5
  • TRAF5 protein, human
  • Transcription Factor RelA