Interaction of atriopeptin III with lipids and detergents

Publisher Website
Google Scholar
Abstract
Atriopeptin III, a potent natural hypotensive agent, contains little α‐helical structure but substantial amounts of β‐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 β‐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 β‐structure.