Interaction of Cyclic Peptides and Depsipeptides with Calmodulin

摘要

A variety of small peptides including hormones, neurotransmitters, and insectvenom components such as ACTH, Beta endorphin, and melittin, respectively, bind calmodulin (CaM) and inhibit CaM-dependent enzyme activity. The binding has been shown to be of high affinity; saturable; calcium dependent; and, upon the removal of calcium, reversible. Peptides bind CaM in either a 1:1 or 1:2 molar ratio and can be competitively displaced from CaM by other non-peptide CaM antagonists such as phenothiazines. Structure-activity studies have demonstrated that most CaM-binding peptides possess either basic amino acids, hydrophobic amino acids, or alpha helical secondary structure. (JES)