Acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) are enzymes that, in humans, are responsible for the hydrolysis of acetylcholine and are therefore investigated as therapeutic targets in the treatment of neurodegenerative diseases associated with a change in the concentration of that neurotransmitter, especially Alzheimer's disease. In this study, eight carbamates with piperidine and pyrrolidine substituents on the nitrogen of the carbamate group were synthesized. The structure of the compounds was characterized by 1H and 13C NMR spectra. For four carbamates whose purity was higher than 85% the ability to inhibit AChE and BChE was determined, and ability to pass the blood-brain barrier evaluated in silico. All compounds proved to be fast or very fast inhibitors of both cholinesterases with inhibition rate constants in the range of 103 -106 mol-1 dm3 min-1. The fastest AChE inhibitors were compounds 8 and 5, piperidine carbamates with a phenylethyl or piperidine substituent at 1- hydroxy-2- aminoethyl chain, respectively, while the fastest BChE inhibitors were compounds 3 (pyrrolidine piperidine monocarbamate with a cyclic pyrrolidine substituent on the 1-hydroxy- 2-aminoethyl chain nitrogen of the carbamate group) and 5. All of the tested carbamates were selective inhibitors of BChE compared to AChE. For the tested carbamates, it was estimated that they can pass through the blood-brain barrier.