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@INPROCEEDINGS{Gutberlet:829769,
author = {Gutberlet, Thomas and Preu, Julia and Tiefenauer, Louis},
title = {{A}dhesion ability of angiotensin {II} with model
membranes},
reportid = {FZJ-2017-03403},
year = {2017},
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 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.},
month = {Mar},
date = {2017-03-19},
organization = {DPG-Frühjahrstagung 2017, Dresden
(Germany), 19 Mar 2017 - 24 Mar 2017},
subtyp = {After Call},
cin = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
(München) ; JCNS-FRM-II},
cid = {I:(DE-Juel1)JCNS-FRM-II-20110218},
pnm = {6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
/ 6G15 - FRM II / MLZ (POF3-6G15)},
pid = {G:(DE-HGF)POF3-6G4 / G:(DE-HGF)POF3-6G15},
experiment = {EXP:(DE-MLZ)External-20140101},
typ = {PUB:(DE-HGF)6},
url = {https://juser.fz-juelich.de/record/829769},
}