Format

Send to

Choose Destination
Bioorg Med Chem Lett. 2010 Feb 1;20(3):1210-3. doi: 10.1016/j.bmcl.2009.11.134. Epub 2009 Dec 4.

Synthesis and biological evaluation of new potential inhibitors of N-acylethanolamine hydrolyzing acid amidase.

Author information

1
Department of Pharmaceutical Sciences, University of Salerno, Via Ponte don Melillo 84084, Fisciano, SA, Italy.

Abstract

N-Acylethanolamines, including N-palmitoyl-ethanolamine (PEA), are hydrolyzed to the corresponding fatty acids and ethanolamine by fatty acid amide hydrolase (FAAH). Recently, N-acylethanolamine-hydrolyzing acid amidase (NAAA) was identified as being able to specifically hydrolyze PEA. In order to find selective and effective inhibitors of this enzyme, we synthesized and screened several amides, retroamides, esters, retroesters and carbamates of palmitic acid (1-21) and esters with C15 and C17 alkyl chains (22-27). Cyclopentylhexadecanoate (13) exhibited the highest inhibitory activity on NAAA (IC(50)=10.0 microM), without inhibiting FAAH up to 50 microM. Compound 13 may become a useful template to design new NAAA inhibitors.

PMID:
20022504
DOI:
10.1016/j.bmcl.2009.11.134
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center