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Serotonin receptors (5-HTRs), especially the 5-HT1A subtype, have been the subject of intensive research for the past decade, due to their function in human physiology. Several structurally different classes of ligands are known to bind to the 5-HT 1A receptor, but arylpiperazine derivatives are among the most important lig- ands. In the work, docking analyses were used to explain the binding affinities of a series of ligands with different N-1 substituent. All ligands had in common the arylpiperazine structure, while the N-1 substituent was modified to investigate the influence of ligand structure on its binding affinity. The shape and size, as well as the rigidity of the substituents were altered to investigate the possible effects on the for- mation of the receptor - ligand complex.

Influence of N-1 substituent properties on binding affinities of arylpiperazines to the binding site of 5-HT1A receptor