<jats:title>Abstract</jats:title><jats:p>Bioassay‐guided fractionation of a collection of <jats:italic>Moorea bouillonii</jats:italic> from Papua New Guinea led to the isolation of a new alkyl amide, mooreamide A (<jats:bold>1</jats:bold>), along with the cytotoxic apratoxins A–C and E. The planar structure of <jats:bold>1</jats:bold> was elucidated by NMR spectroscopy and mass spectrometry analysis. Structural homology between mooreamide A and the endogenous cannabinoid ligands, anandamide, and 2‐arachidonoyl glycerol inspired its evaluation against the neuroreceptors CB<jats:sub>1</jats:sub> and CB<jats:sub>2</jats:sub>. Mooreamide A was found to possess relatively potent and selective ligand binding activity to CB<jats:sub>1</jats:sub> (<jats:italic>K</jats:italic><jats:sub>1</jats:sub> = 0.47 µM) versus CB<jats:sub>2</jats:sub> (<jats:italic>K</jats:italic><jats:sub>1</jats:sub> > 25 µM). This represents the most potent marine‐derived CB<jats:sub>1</jats:sub> ligand described to date and adds to the growing family of marine metabolites that exhibit cannabinomimetic activity.