A series of hybrid molecules between (${alpha}$)-lipoic acid (ALA) and 4-amino-1-benzyl piperidines were synthesized and their in vitro cholinesterase (acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE)) inhibitory activities were evaluated. Even though the parent compounds did not exhibit any inhibitory activity against cholinesterase (ChE) with the exception of compound 14 ($IC_{50}=255.26{pm}4.41$ against BuChE), all hybrid molecules demonstrated BuChE inhibitory activity. Some hybrid compounds also displayed AChE inhibitory activity. Specifically, compound 17 was shown to be an effective inhibitor against both AChE ($IC_{50}=1.75{pm}0.30{mu}M$) and BuChE ($IC_{50}=5.61{pm}1.25{mu}M$) comparable to galantamine ($IC_{50}=1.7{pm}0.9{mu}M$ against AChE and $IC_{50}=9.4{pm}2.5{mu}M$ against BuChE). Inhibition kinetic studies using compound 17 indicated a mixed inhibition type for AChE and a noncompetitive inhibition type for BuChE. Its binding affinity ($K_i$) values to AChE and BuChE were $3.8{pm}0.005{mu}M$ and $7.0{pm}0.04{mu}M$, respectively.