The hydrophobic moment of the amphipathic helix of salmon calcitonin and biological potency.
The formation of an amphipathic helix in the central portion of calcitonin contributes to the potency of this hormone. We have synthesized a number of analogs of salmon calcitonin, containing deletions in the region of the peptide which is thought to form an amphipathic helix. There is no direct relationship between the hydrophobic moment of the helix and the biological activity of the peptide. For example, salmon des-Leu19-calcitonin and des-Ser13-calcitonin both have lower helical hydrophobic moments but have greater or equal biological potency compared with the native hormone. We suggest that other conformational features, such as flexibility and helix-forming potential, are also important in determining biological potency.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002116:Calcitonin; D002942:Circular Dichroism; D010446:Peptide Fragments / Q000032:analysis; D011487:Protein Conformation; D012995:Solubility
D000596:Amino Acids; D010446:Peptide Fragments; C028815:salmon calcitonin; D002116:Calcitonin