In Vitro Assay Development and HTS of Small-Molecule Human ABAD/17β-HSD10 Inhibitors as Therapeutics in Alzheimer's Disease

SLAS Discov. 2017 Jul;22(6):676-685. doi: 10.1177/2472555217697964. Epub 2017 Mar 17.

Abstract

A major hallmark of Alzheimer's disease (AD) is the formation of neurotoxic aggregates composed of the amyloid-β peptide (Aβ). Aβ has been recognized to interact with numerous proteins, resulting in pathological changes to the metabolism of patients with AD. One such mitochondrial metabolic enzyme is amyloid-binding alcohol dehydrogenase (ABAD), where altered enzyme function caused by the Aβ-ABAD interaction is known to cause mitochondrial distress and cytotoxic effects, providing a feasible therapeutic target for AD drug development. Here we have established a high-throughput screening platform for the identification of modulators to the ABAD enzyme. A pilot screen with a total of 6759 compounds from the NIH Clinical Collections (NCC) and SelleckChem libraries and a selection of compounds from the BioAscent diversity collection have allowed validation and robustness to be optimized. The pilot screen revealed 16 potential inhibitors in the low µM range against ABAD with favorable physicochemical properties for blood-brain barrier penetration.

Keywords: enzyme assays or enzyme kinetics; ligand binding; neurodegenerative diseases; pharmacology; receptor binding; ultra-high-throughput screening.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3-Hydroxyacyl CoA Dehydrogenases / antagonists & inhibitors*
  • Alzheimer Disease / drug therapy
  • Chemical Phenomena
  • Drug Discovery* / methods
  • Enzyme Assays* / methods
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / pharmacology*
  • Enzyme Inhibitors / therapeutic use
  • High-Throughput Screening Assays*
  • Humans
  • In Vitro Techniques
  • Kinetics
  • Ligands
  • Protein Binding
  • Reproducibility of Results

Substances

  • Enzyme Inhibitors
  • Ligands
  • 3-Hydroxyacyl CoA Dehydrogenases
  • HSD17B10 protein, human