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@ARTICLE{Preu:823897,
      author       = {Preu, Julia and Tiefenauer, Louis and Gutberlet, Thomas},
      title        = {{A}dhesion ability of angiotensin {II} with model
                      membranes},
      journal      = {Biochimica et biophysica acta / Biomembranes},
      volume       = {1859},
      issn         = {0005-2736},
      address      = {Amsterdam},
      publisher    = {Elsevier},
      reportid     = {FZJ-2016-06529},
      pages        = {195},
      year         = {2016},
      abstract     = {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 regulation in
                      mammals.Predominantly binding to the Angiotensin type 1 and
                      2 receptors, the hormone is oneof several peptide ligands
                      binding to G protein coupled receptors (GPCR). The
                      activehormone derives from a high molecular weight precursor
                      sequentially cleaved by theproteases renin and the
                      angiotensin converting enzyme (ACE). The chemical natureof
                      the amino acid sequence has an impact on the behavior in the
                      proximity ofmembranes, demonstrated using different membrane
                      model systems and biophysicalmethods.Applying
                      electrochemical impedance spectroscopy and small angle x-ray
                      scattering adetailed view on the adhesion of the peptide
                      with model membrane surfaces wasperformed. The role of
                      specific amino acids involved in the interaction with
                      thephospholipid head group were investigated and, studying a
                      truncated version of AngII, Ang (1-7), the key role of the
                      C-terminal phenylalanine was proven. Truncation ofthe
                      C-terminal amino acid abolishes the binding of the peptide
                      to the membranesurface. A shift in pH, altering the
                      protonation state of the central histidine residueimpairs
                      the adhesion of Ang II.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1 /
                      JCNS-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)JCNS-2-20110106},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621) /
                      6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)},
      pid          = {G:(DE-HGF)POF3-6215 / G:(DE-HGF)POF3-6G4},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000392772100006},
      pubmed       = {pmid:27865700},
      doi          = {10.1016/j.bbamem.2016.11.007},
      url          = {https://juser.fz-juelich.de/record/823897},
}