AM 1172 is a potent and selective inhibitor of stable anandamide uptake with IC50 of 2.1 - 2.5 μM and fatty acid amide hydrolase (FAAH) with Ki of 3.18 μM.

FAAH, a member of serine hydrolase enzyme family, is an integral membrane hydrolase that hydrolyzes bioactive amides, including anandamide, to free fatty acid and ethanolamine. In vitro, FAAH displays esterase and amidase activity. In vivo, this protein acts as the principal catabolic enzyme for a class of bioactive lipids called the fatty acid amides (FAAs).

AM1172 blocked [3H] anandamide internalization in rodent cortical neurons and human astrocytoma cells but not acted as an inhibitor of FAAH 1. In mouse cortical neurons, This component also blocked the uptake of tritiated AEA with an EC50 of about 1.5 μM 1.

Regarding the effect of AM 1172 administration in vivo, the evidence should be provided by performing the study in human or mice or other animal models.

Reference:
1.  Fegley D, Kathuria S, Mercier R, et al. Anandamide transport is independent of fatty-acid amide hydrolase activity and is blocked by the hydrolysis-resistant inhibitor AM1172. Proceedings of the National Academy of Sciences of the United States of America. 2004;101(23):8756-8761.