The 26-residue peptide melittin present in bee venom has been shown to bind calmodulin tightly. In this study we synthesized the following series of deletion peptides of melittin by the solid-phase method: Mel12, Mel13, Mel14, Mel15, Mel15F. The results of this study show that the deletion peptides Mel14 and Mel15 have almost the same binding activity as the intact native peptide. Each deletion peptide forms a 1:1 complex with calmodulin according to electrophoresis analysis. When the tryptophanyl residue of Mel15 was replaced by the phenylalaninyl residue, the dissociation constant of the peptide-calmodulin complex increased. This shows the importance of the tryptophanyl residue for binding to calmodulin.