000823897 001__ 823897 000823897 005__ 20210129224901.0 000823897 0247_ $$2doi$$a10.1016/j.bbamem.2016.11.007 000823897 0247_ $$2WOS$$aWOS:000392772100006 000823897 0247_ $$2altmetric$$aaltmetric:15233519 000823897 0247_ $$2pmid$$apmid:27865700 000823897 037__ $$aFZJ-2016-06529 000823897 041__ $$aEnglish 000823897 082__ $$a570 000823897 1001_ $$0P:(DE-HGF)0$$aPreu, Julia$$b0$$eCorresponding author 000823897 245__ $$aAdhesion ability of angiotensin II with model membranes 000823897 260__ $$aAmsterdam$$bElsevier$$c2016 000823897 3367_ $$2DRIVER$$aarticle 000823897 3367_ $$2DataCite$$aOutput Types/Journal article 000823897 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1488881523_24234 000823897 3367_ $$2BibTeX$$aARTICLE 000823897 3367_ $$2ORCID$$aJOURNAL_ARTICLE 000823897 3367_ $$00$$2EndNote$$aJournal Article 000823897 520__ $$aThe 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. 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