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@ARTICLE{Nielsen:889770,
author = {Nielsen, Josefine Eilsø and Bjørnestad, Victoria Ariel
and Pipich, Vitaliy and Jenssen, Håvard and Lund, Reidar},
title = {{B}eyond structural models for the mode of action: {H}ow
natural antimicrobial peptides affect lipid transport},
journal = {Journal of colloid and interface science},
volume = {582},
number = {Part B},
issn = {0021-9797},
address = {Amsterdam [u.a.]},
publisher = {Elsevier},
reportid = {FZJ-2021-00383},
pages = {793 - 802},
year = {2021},
abstract = {Hypothesis: Most textbook models for antimicrobial peptides
(AMP) mode of action are focused on structural effects and
pore formation in lipid membranes, while these deformations
have been shown to require high concentrations of peptide
bound to the membrane. Even insertion of low amounts of
peptides in the membrane is hypothesized to affect the
transmembrane transport of lipids, which may play a key role
in the peptide effect on membranes. Experiments: Here we
combine state-of-the-art small angle X-ray/neutron
scattering (SAXS/SANS) techniques to systematically study
the effect of a broad selection of natural AMPs on lipid
membranes. Our approach enables us to relate the structural
interactions, effects on lipid exchange processes, and
thermodynamic parameters, directly in the same model system.
Findings: The studied peptides, indolicidin, aurein 1.2,
magainin II, cecropin A and LL-37 all cause a general
acceleration of essential lipid transport processes, without
necessarily altering the overall structure of the lipid
membranes or creating organized pore-like structures. We
observe rapid scrambling of the lipid composition associated
with enhanced lipid transport which may trigger lethal
signaling processes and enhance ion transport. The reported
membrane effects provide a plausible canonical mechanism of
AMP-membrane interaction and can reconcile many of the
previously observed effects of AMPs on bacterial membranes.},
cin = {JCNS-4 / JCNS-1 / JCNS-FRM-II / MLZ},
ddc = {540},
cid = {I:(DE-Juel1)JCNS-4-20201012 / I:(DE-Juel1)JCNS-1-20110106 /
I:(DE-Juel1)JCNS-FRM-II-20110218 / I:(DE-588b)4597118-3},
pnm = {6215 - Soft Matter, Health and Life Sciences (POF3-621) /
6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
/ 6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
Neutron Research (JCNS) (FZJ) (POF4-6G4) / 632 - Materials
– Quantum, Complex and Functional Materials (POF4-632)},
pid = {G:(DE-HGF)POF3-6215 / G:(DE-HGF)POF3-6G4 /
G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF4-6G4 /
G:(DE-HGF)POF4-632},
experiment = {EXP:(DE-MLZ)KWS2-20140101 / EXP:(DE-MLZ)KWS3-20140101},
typ = {PUB:(DE-HGF)16},
pubmed = {32911421},
UT = {WOS:000600666100002},
doi = {10.1016/j.jcis.2020.08.094},
url = {https://juser.fz-juelich.de/record/889770},
}