A simplified scintillation proximity assay for fatty acid synthase activity: development and comparison with other FAS activity assays

J Biomol Screen. 2009 Jul;14(6):636-42. doi: 10.1177/1087057109335746. Epub 2009 Jun 16.

Abstract

Fatty acid synthase (FAS), an essential enzyme for de novo lipogenesis, has been implicated in a number of disease states, including obesity, dyslipidemia, and cancer. To identify small-molecule inhibitors of FAS, the authors developed a bead-based scintillation proximity assay (SPA) to detect the fatty acid products of FAS enzymatic activity. This homogeneous SPA assay discriminates between a radiolabeled hydrophilic substrate of FAS (acetyl-coenzyme A) and the labeled lipophilic products of FAS (fatty acids), generating signal only when labeled fatty acids are present. The assay requires a single addition of unmodified polystyrene imaging SPA beads and can be miniaturized to 384- or 1536-well density with appropriate assay statistics for high-throughput screening. High-potency FAS inhibitors were used to compare the sensitivity of the SPA bead assay with previously described assays that measure FAS reaction intermediates (CoA-SH and NADP+). The advantages and disadvantages of these different FAS assays in small-molecule inhibitor discovery are discussed.

Publication types

  • Comparative Study

MeSH terms

  • Acetyl Coenzyme A / metabolism
  • Biological Assay / methods*
  • Cell Line
  • Fatty Acid Synthases / antagonists & inhibitors
  • Fatty Acid Synthases / metabolism*
  • Humans
  • NADP / metabolism
  • Palmitates / metabolism
  • Signal Transduction
  • Time Factors
  • Titrimetry

Substances

  • Palmitates
  • NADP
  • Acetyl Coenzyme A
  • Fatty Acid Synthases