A Potent Systemically Active <i>N</i>-Acylethanolamine Acid Amidase Inhibitor that Suppresses Inflammation and Human Macrophage Activation

Alison Ribeiro, Silvia Pontis, Luisa Mengatto, Andrea Armirotti, Valerio Chiurchiù, Valeria Capurro, Annalisa Fiasella, Andrea Nuzzi, Elisa Romeo, Guillermo Moreno‐Sanz,

ACS Chemical Biology · 2015 · 76 citations · 18 references

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Abstract

Fatty acid ethanolamides such as palmitoylethanolamide (PEA) and oleoylethanolamide (OEA) are lipid-derived mediators that potently inhibit pain and inflammation by ligating type-α peroxisome proliferator-activated receptors (PPAR-α). These bioactive substances are preferentially degraded by the cysteine hydrolase, N-acylethanolamine acid amidase (NAAA), which is highly expressed in macrophages. Here, we describe a new class of β-lactam derivatives that are potent, selective, and systemically active inhibitors of intracellular NAAA activity. The prototype of this class deactivates NAAA by covalently binding the enzyme's catalytic cysteine and exerts profound anti-inflammatory effects in both mouse models and human macrophages. This agent may be used to probe the functions of NAAA in health and disease and as a starting point to discover better anti-inflammatory drugs.

References

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