title: Adhesion ability of angiotensin II with model membranes.
abstract: The octa-peptide angiotensin II (Ang II, (H2NAspArgValTyrIleHisProPheCOOH)) is one of the key player on blood pressure regulation in mammals. Predominantly binding to the Angiotensin type 1 and 2 receptors, the hormone is one of several peptide ligands binding to G protein coupled receptors (GPCR). The active hormone derives from a high molecular weight precursor sequentially cleaved by the proteases renin and the angiotensin converting enzyme (ACE). The chemical nature of the amino acid sequence has an impact on the behavior in the proximity of membranes, demonstrated using different membrane model systems and biophysical methods. Applying electrochemical impedance spectroscopy and small angle X-ray scattering a detailed view on the adhesion of the peptide with model membrane surfaces was performed. The role of specific amino acids involved in the interaction with the phospholipid head group were investigated and, studying a truncated version of Ang II, Ang (1-7), the key role of the C-terminal phenylalanine was proven. Truncation of the C-terminal amino acid abolishes the binding of the peptide to the membrane surface. A shift in pH, altering the protonation state of the central histidine residue impairs the adhesion of Ang II.
authors.affiliation: Membrane Biophysics Group, Niels Bohr Institute, University of Copenhagen, Copenhagen, Denmark. Electronic address: Julia.Preu@virchow.uni-wuerzburg.de.
authors.forename: Julia
authors.initials: J
authors.lastname: Preu
authors.affiliation: Laboratory of Biomolecular Research, Paul Scherrer Institut, Villigen PSI, Switzerland.
authors.forename: Louis
authors.initials: L
authors.lastname: Tiefenauer
authors.affiliation: Jülich Centre for Neutron Science at Heinz Maier-Leibnitz Zentrum, Forschungszentrum Jülich GmbH, Garching, Germany.
authors.forename: Thomas
authors.initials: T
authors.lastname: Gutberlet
mesh_terms: D000596:Amino Acids / Q000378:metabolism; D000803:Angiotensin I / Q000378:metabolism; D000804:Angiotensin II / Q000378:metabolism*; D001665:Binding Sites / Q000502:physiology; D006639:Histidine / Q000378:metabolism; D006801:Humans; D008566:Membranes / Q000378:metabolism*; D008970:Molecular Weight; D010446:Peptide Fragments / Q000378:metabolism; D010455:Peptides / Q000378:metabolism; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism; D010649:Phenylalanine / Q000378:metabolism; D011485:Protein Binding / Q000502:physiology; D044140:Receptor, Angiotensin, Type 1 / Q000378:metabolism; D044139:Receptor, Angiotensin, Type 2 / Q000378:metabolism; D043562:Receptors, G-Protein-Coupled / Q000378:metabolism; D012083:Renin / Q000378:metabolism; D012084:Renin-Angiotensin System / Q000502:physiology
chemical_list: D000596:Amino Acids; D010446:Peptide Fragments; D010455:Peptides; D044140:Receptor, Angiotensin, Type 1; D044139:Receptor, Angiotensin, Type 2; D043562:Receptors, G-Protein-Coupled; D000804:Angiotensin II; D010649:Phenylalanine; D006639:Histidine; D000803:Angiotensin I; D007703:Peptidyl-Dipeptidase A; D012083:Renin; C118790:angiotensin I (1-7)