Interaction of atriopeptin III with lipids and detergents.
Atriopeptin III, a potent natural hypotensive agent, contains little alpha-helical structure but substantial amounts of beta-structure. The peptide can self-associate at millimolar concentrations or can associate with the anionic phospholipid, dimyristoylphosphatidylglycerol. Both of these processes are accompanied by a conformational change suggesting the formation of an increased amount of beta-structure. The peptide can broaden the transition and lower the transition enthalpy of dimyristoylphosphatidylglycerol. The results demonstrate that a peptide hormone can associate with lipid largely in the form of a beta-structure.
D009320:Atrial Natriuretic Factor; D002152:Calorimetry, Differential Scanning; D002942:Circular Dichroism; D004134:Dimyristoylphosphatidylcholine; D008244:Lysophosphatidylcholines; D008968:Molecular Conformation; D010715:Phosphatidylglycerols; D011487:Protein Conformation; D012967:Sodium Dodecyl Sulfate
D008244:Lysophosphatidylcholines; D010715:Phosphatidylglycerols; D012967:Sodium Dodecyl Sulfate; D009320:Atrial Natriuretic Factor; C002773:dimyristoylphosphatidylglycerol; D004134:Dimyristoylphosphatidylcholine