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000889770 1001_ $$0P:(DE-HGF)0$$aNielsen, Josefine Eilsø$$b0
000889770 245__ $$aBeyond structural models for the mode of action: How natural antimicrobial peptides affect lipid transport
000889770 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2021
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000889770 520__ $$aHypothesis: 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.
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000889770 7001_ $$0P:(DE-HGF)0$$aBjørnestad, Victoria Ariel$$b1
000889770 7001_ $$0P:(DE-Juel1)130893$$aPipich, Vitaliy$$b2
000889770 7001_ $$0P:(DE-HGF)0$$aJenssen, Håvard$$b3
000889770 7001_ $$00000-0001-8017-6396$$aLund, Reidar$$b4$$eCorresponding author
000889770 773__ $$0PERI:(DE-600)1469021-4$$a10.1016/j.jcis.2020.08.094$$gVol. 582, p. 793 - 802$$nPart B$$p793 - 802$$tJournal of colloid and interface science$$v582$$x0021-9797$$y2021
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