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A binding site for nonsteroidal anti-inflammatory drugs in fatty acid amide hydrolase

  • Author(s): Bertolacci, L
  • Romeo, E
  • Veronesi, M
  • Magotti, P
  • Albani, C
  • Dionisi, M
  • Lambruschini, C
  • Scarpelli, R
  • Cavalli, A
  • De Vivo, M
  • Piomelli, D
  • Garau, G
  • et al.

Published Web Location

https://doi.org/10.1021/ja308733uCreative Commons Attribution 4.0 International Public License
Abstract

In addition to inhibiting the cyclooxygenase (COX)-mediated biosynthesis of prostanoids, various widely used nonsteroidal anti-inflammatory drugs (NSAIDs) enhance endocannabinoid signaling by blocking the anandamide-degrading membrane enzyme fatty acid amide hydrolase (FAAH). The X-ray structure of FAAH in complex with the NSAID carprofen, along with site-directed mutagenesis, enzyme activity assays, and NMR analysis, has revealed the molecular details of this interaction, providing information that may guide the design of dual FAAH-COX inhibitors with superior analgesic efficacy. © 2012 American Chemical Society.

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