A library of artificial receptors formed by the self-organization of N-lipidated peptides attached to cellulose via m-aminophenylamino-1,3,5-triazine was used for docking pairs of small colorless N-phenylpiperazines with and without a fluorine atom in the phenyl ring. The interactions of guests with the receptors were visualized by using competitive adsorption-desorption of an appropriate reporter dye. Several library members demonstrated attributes characteristic of the detection of alterations in the guest structure caused by the substitution of one hydrogen atom with fluorine. Analysis of the binding pattern of N-phenylpiperazine derivatives showed two characteristic bonding patterns: one with stronger binding of fluorinated analogues and weaker binding of native phenyl substituted analogues by the most of the receptors studied and another one with stronger binding of native hydrogen substituted compounds and respectively weaker binding of fluorinated analogues of guest molecules by receptors with tryptophan inside the binding pocket.