Epand R M, Epand R F, Hui S W, He N B, Rosenblatt M
Int J Pept Protein Res. 1985 Jun;25(6):594-600. doi: 10.1111/j.1399-3011.1985.tb02215.x.
Two biologically active, 34 amino acid fragments of parathyroid hormone interact with dimyristoylphosphatidylcholine to form lipoprotein particles. In the lipid-bound form these parathyroid hormone peptides exhibit an increased amount of folded secondary structure and the tryptophan residue of [Nle8, Nle18, Tyr34] b PTH (1-34) amide appears to become buried in a more hydrophobic environment. The lipoprotein particle which is formed has dimensions of approximately 65 X 7 nm but aggregates to larger structures with increasing temperature. Above the phase transition of the phospholipid the peptides no longer affect the morphology of the lipid and the spectral properties of the peptide are not perturbed by the lipid. This is similar to the behavior of glucagon with dimyristoylphatidylcholine. The results indicate that several nonhomologous peptide hormones have common features which allow them to fold into an amphipathic helix and solubilize phospholipid.
甲状旁腺激素的两个具有生物活性的34个氨基酸片段与二肉豆蔻酰磷脂酰胆碱相互作用形成脂蛋白颗粒。以脂质结合形式存在时，这些甲状旁腺激素肽呈现出增加的折叠二级结构量，并且[Nle8，Nle18，Tyr34] b PTH（1-34）酰胺的色氨酸残基似乎被埋在更疏水的环境中。形成的脂蛋白颗粒尺寸约为65×7nm，但随着温度升高会聚集形成更大的结构。在磷脂的相变温度以上，这些肽不再影响脂质的形态，并且肽的光谱特性也不会受到脂质的干扰。这与胰高血糖素与二肉豆蔻酰磷脂酰胆碱的行为相似。结果表明，几种非同源肽激素具有共同特征，使它们能够折叠成两亲性螺旋并溶解磷脂。
