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Exceptionally potent inhibitors of fatty acid amide hydrolase: the enzyme responsible for degradation of endogenous oleamide and anandamide

Academic Article
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Overview

related to degree

  • Wilkie, Gordon, Ph.D. in Chemistry, Scripps Research 1997 - 2002
  • Patricelli, Matt, Ph.D. in Biology, Scripps Research 1996 - 2000

authors

  • Boger, Dale
  • Sato, H.
  • Lerner, A. E.
  • Hedrick, M. P.
  • Fecik, R. A.
  • Miyauchi, H.
  • Wilkie, Gordon
  • Austin, B. J.
  • Patricelli, Matt
  • Cravatt, Benjamin

publication date

  • May 2000

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • The development of exceptionally potent inhibitors of fatty acid amide hydrolase (FAAH), the enzyme responsible for the degradation of oleamide (an endogenous sleep-inducing lipid), and anandamide (an endogenous ligand for cannabinoid receptors) is detailed. The inhibitors may serve as useful tools to clarify the role of endogenous oleamide and anandamide and may prove to be useful therapeutic agents for the treatment of sleep disorders or pain. The combination of several features-an optimal C12-C8 chain length, pi-unsaturation introduction at the corresponding arachidonoyl Delta(8,9)/Delta(11,12) and oleoyl Delta(9,10) location, and an alpha-keto N4 oxazolopyridine with incorporation of a second weakly basic nitrogen provided FAAH inhibitors with K(i)s that drop below 200 pM and are 10(2)-10(3) times more potent than the corresponding trifluoromethyl ketones.

subject areas

  • Amidohydrolases
  • Animals
  • Arachidonic Acids
  • COS Cells
  • Cannabinoids
  • Cell Membrane
  • Cerebrosides
  • Drug Design
  • Endocannabinoids
  • Enzyme Inhibitors
  • Heterocyclic Compounds
  • Kinetics
  • Liver
  • Oleic Acids
  • Polyunsaturated Alkamides
  • Rats
  • Recombinant Proteins
  • Structure-Activity Relationship
  • Transfection
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Identity

PubMed Central ID

  • PMC25778

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.97.10.5044

PubMed ID

  • 10805767
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Additional Document Info

start page

  • 5044

end page

  • 5049

volume

  • 97

issue

  • 10

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