Formation of water‐soluble complex between the 1–34 fragment of parathyroid hormone and dimyristoylphosphatidylcholine

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Abstract
Two biologically active, 34 amino acid fragments of parathyroid hormone interact with dimyristolyphosphatidylcholine to form lipoprotein particles. In the lipid-bound form these parathyroid hormone [PTH] peptides exhibit an increased amount of folded secondary structure and tryptophan residue of [Nle8, Nle18, Tyr34] b [bovine] PTH (1-34) amide appears to become buried in a more hydrophobic environment. The lipoprotion particle which is formed has dimensions of approximately 65 .times. 7 nm but aggregates to larger structures with increasing temperature. Above the phase transition of the phsopholipid 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 dimyristoylphosphatidylcholine. Several non-homologous peptide hormones have common features which allow them to fold into an amphipathic helix and solubilize phospholipid.