Adhesion ability of angiotensin II with model membranes

The octa-peptide angiotensin II (Ang II, (H2N-Asp*Arg*Val*Tyr*Ile*His*Pro*Phe*COOH)) is one of the key player on blood pressure regulationin mammals. Predominantly binding to the Angiotensin type 1and 2 receptors, the hormone is one of several peptide ligands bindingto G protein coupled receptors (GPCR). The chemical nature of theamino acid sequence has an impact on the behavior in the proximityof membranes, demonstrated using different membrane model systemsand biophysical methods. Applying electrochemical impedance spectroscopyand small angle x-ray scattering a detailed view on the adhesionof the peptide with model membrane surfaces was performed.The role of specific amino acids involved in the interaction with thephospholipid head group were investigated and, studying a truncatedversion of Ang II, Ang (1-7), the key role of the C-terminal phenylalaninewas proven