In addition to the well-known acetylcholinesterase (AChE), another enzyme can terminate cholinergic transmission in the human body: human butyrylcholinesterase (hBChE). Due to its lower substrate specificity, hBChE can hydrolyse a number of different esterse.g., hungerhormone ghrelin, cocaine and heroin, among others, although its precise physiological role still remains a mystery. Over the last three decades, BChE has emerged as an interesting and wellexplored target in the medicinal chemistry community, especially in the fields of neurodegenerative diseases (predominantly Alzheimer's disease), bioscavanging organophosphorous nerve agents, inactivation of cocaine, heroin overdose prevention, and ghrelin-mediated effects on body weight. The BChE active site can be separated into several defined regions: the catalytic triad (Ser198, His438, Glu325); the oxyanion hole (Gly116, Gly117, Ala199); the choline-binding pocket (Trp82); and the acyl-binding pocket (Trp231, Leu286, Val288, Phe329). Near the entrance to the active site gorge there is the putative peripheral site, made of residues Asp70 and Tyr332. Leaving a superabundance of classic reversible BChE inhibitors (BChEIs) aside, different cholinesterase inhibitor (ChEI) classes that feature carbamate moieties have been reported in the literaturee.g., Scheme 1: derivatives of physostigmine (1a,), isosorbide, tetrahydroquinazoline (1b, 1d), phenothiazine, xanthone, chalcone, coumarin, resveratrol, Nsubstituted piperidine and piperazine, indole (1c), and others; these were well-covered in a recent review that highlighted their potential multifunctionality. Furthermore, the first ChEI discovered was indeed the plant alkaloid physostigmine 1a, where its covalent pseudoirreversible mechanism of action through a carbamate warhead was only later realised. Scheme 1: Representative carbamate cholinesterase inhibitors from the literature.