Epand R M, Seyler J K, Orlowski R C
Eur J Biochem. 1986 Aug 15;159(1):125-7. doi: 10.1111/j.1432-1033.1986.tb09841.x.
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.
降钙素中央部分两亲性螺旋的形成有助于该激素的效力。我们合成了许多鲑鱼降钙素类似物，这些类似物在被认为形成两亲性螺旋的肽区域存在缺失。螺旋的疏水矩与肽的生物活性之间没有直接关系。例如，鲑鱼去亮氨酸-19-降钙素和去丝氨酸-13-降钙素的螺旋疏水矩都较低，但与天然激素相比，它们具有更高或相等的生物效力。我们认为，其他构象特征，如柔韧性和形成螺旋的潜力，在决定生物效力方面也很重要。
