Butyrylcholinesterase is one of the key enzymes in the regulation of the neurotransmitter acetylcholine and in the metabolism of non-choline esters. The role of butyrylcholinesterase is to hydrolyse ester bonds, which in the case of acetylcholine, causes the termination of cholinergic synaptic signalization. The overexpression of the enzyme causes a serious decrease in cerebral acetylcholine signalization, which in turn can affect the ability of the brain to generate new memories. This is what happens during the progression of certain types of dementia, such as Alzheimer's disease. Aside from the overregulation of cerebral acetylcholine, butyrylcholinesterase correlates with other Alzheimer's disease pathologies, such as the accumulation of protein plaques. Because of the pathological increase of the enzyme during the progression of Alzheimer's disease, scientists have been trying for decades to develop drugs that would inhibit butyrylcholinesterase activity and alleviate the symptoms of the disease. Four out of five therapeutical agents that are currently available for the treatment of Alzheimer's dementia are cholinesterase inhibitors. Because there are currently no available drugs that could successfully directly target brain plaque accumulation, cholinesterase inhibitors are the most promising drugs for treating dementia on the market. The goal of this diploma was to synthesize and in vitro test two new potential butyrylcholinesterase inhibitors. The base for the new inhibitors was the amino acid tryptophan to which we successfully added a 2-cyclheptylethanamino group (C-terminus) as well as a benzyl/butyryl group (N-terminus). We tested the inhibitory strength of both compounds in a kinetic test with human butyrylcholinesterase and they both inhibited the enzyme in the nanomolar range.