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Cover Picture: Structure–Property Relationships of a Class of Carbamate‐Based Fatty Acid Amide Hydrolase (FAAH) Inhibitors: Chemical and Biological Stability / A Second Generation of Carbamate‐Based Fatty Acid Amide Hydrolase Inhibitors with Improved Activity in vivo (ChemMedChem 9/2009)
Author(s) -
Vacondio Federica,
Silva Claudia,
Lodola Alessio,
Fioni Alessandro,
Rivara Silvia,
Duranti Andrea,
Tontini Andrea,
Sanchini Silvano,
Clapper Jason R.,
Piomelli Daniele,
Mor Marco,
Tarzia Giorgio,
King Alvin R.
Publication year - 2009
Publication title -
chemmedchem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.200990041
Subject(s) - fatty acid amide hydrolase , anandamide , chemistry , serine hydrolase , hydrolase , carbamate , stereochemistry , biochemistry , serine , enzyme , amidase , fatty acid , active site , amide , cannabinoid receptor , receptor , agonist
The cover picture shows two carbamate‐based inhibitors of fatty acid amide hydrolase (FAAH), the enzyme responsible for the catalysis of the endocannabinoid anandamide hydrolysis. URB597 (purple) is hydrolyzed in plasma and may modify other serine hydrolases, leading to unwanted side effects. Chemical modifications of URB597 resulted in the identification of URB694 (white), which has improved plasma stability, lower propensity to inhibit liver esterases and higher potency when administered in vivo. URB694 is shown here in the active site of FAAH; both compounds inhibit this enzyme through serine carbamoylation. For more details, see the Full Papers by M. Mor and D. Piomelli et al. on p. 1495 ff. and p. 1505 ff.