Biological activities and receptor interactions of des-Leu16 salmon and des-Phe16 human calcitonin

Abstract

Analogs of salmon (des-Leu16 sCT) and human (des-Phe16 hCT) calcitonin were prepared in which the amino acid from position 16 was omitted. The biological activities were assessed in vivo in the rat hypocalcemic assay and in vitro by studying competition for binding of [125I]sCT and adenylate cyclase stimulation in human breast cancer cells (T 47D). Deletion from position 16 resulted in substantial loss of biological activity in each system, indicating the importance for a hydrophobic residue at position 16 in the intact calcitonin molecule.