Synthesis of the fragments of melittin and their interaction with calmodulin

Four fragments of melittin were manually synthesized by standard solid-phase method: Mel 12, Mel 13, Mel 14 and Mel 15. Their interaction with calmodulin was studied by electrophoresis method, inhibited activity of Ca~(2+)-dependent 3^,5^-cAMP phosphodiesterase and flurescence technique. The results show that these peptides form 1:1 complex with calmodulin and inhibit the activity of phosphodiesterase. Among these peptides, Mel 14 and Mel 15 have almost the same binding activity with calmodulin as the intact peptide Melittin.