Interaction of atriopeptin III with lipids and detergents
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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.
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