Two new somatostatin analogs with a characteristic part of the sequence -c(Cys-Phe-Trp-Lys-Thr-Cys)- and with two histidine and two aspartic acid moieties in their structures were synthesized and analyzed in terms of their coordination abilities with copper (II) ions. Both peptides bind Cu(II) effectively. Ligands form 4N complexes with \(\left\{ {{\text{N}}_{\text{Im}} ,{ 3} {\text{N}}_{\text{amide}}^{ - } } \right\}\) binding mode in a basic range of pH. But in spite of very similar sequences of the two peptides a significant difference in the effectiveness of the binding of copper (II) ions was observed.