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001034425 0247_ $$2doi$$a10.1016/j.molliq.2024.126086
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001034425 1001_ $$00000-0003-3389-6942$$aVitiello, Giuseppe$$b0$$eCorresponding author
001034425 245__ $$aThe affinity towards the hydrophobic region of biomimicking bacterial membranes drives the antimicrobial activity of EFV12 peptide from Lactobacillus gasseri gut microbiota
001034425 260__ $$aNew York, NY [u.a.]$$bElsevier$$c2024
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001034425 520__ $$aThe gut microbiota consists of a large variety of microorganisms, which interact with the immune system and exert essential roles for the human body health. Many of these microorganisms are also capable of producing various bioactive molecules, such as selective antimicrobial peptides, thus promoting the proliferation of only certain bacterial strains. These result in the shaping of the composition of the local microbiome and the co-evolution with a complex microbiome. Recently, a small peptide, named EFV12 and deriving from the bacterium Lactobacillus gasseri SF1109 regularly placed in the human intestine, showed a significant antimicrobial activity. Here we discuss a biophysical study on the structural changes induced by the peptide on lipid bilayers mimicking bacterial membranes with the aim of shedding light on the molecular features driving the biocidal activity against Gram(+) and Gram(−) strains. Supported Lipid Bilayers and liposomes composed of 1,2-oleoyl-sn-glycero-3-phosphocholine and 1,2-oleoyl-sn-glycero-3-rac-phosphoglycerol, both in the absence and presence of cardiolipin and lipopolysaccharides (LPSs), were selected to investigate the peptide-lipid interactions through a combination of specular Neutron Reflectometry, Dynamic Light Scattering, Small-Angle X-ray Scattering and Circular Dichroism measurements. The obtained results indicated association of EFV12 peptide with the hydrophobic region of lipid bilayers, which caused their destabilization, and is thus driving the antimicrobial activity against bacterial cells.
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001034425 65027 $$0V:(DE-MLZ)SciArea-160$$2V:(DE-HGF)$$aBiology$$x0
001034425 65017 $$0V:(DE-MLZ)GC-130-2016$$2V:(DE-HGF)$$aHealth and Life$$x0
001034425 693__ $$0EXP:(DE-MLZ)MARIA-20140101$$1EXP:(DE-MLZ)FRMII-20140101$$5EXP:(DE-MLZ)MARIA-20140101$$6EXP:(DE-MLZ)NL5N-20140101$$aForschungs-Neutronenquelle Heinz Maier-Leibnitz $$eMARIA: Magnetic reflectometer with high incident angle$$fNL5N$$x0
001034425 7001_ $$00000-0003-2380-6069$$aLuchini, Alessandra$$b1
001034425 7001_ $$0P:(DE-HGF)0$$aDi Napoli, Michela$$b2
001034425 7001_ $$0P:(DE-HGF)0$$aGallucci, Noemi$$b3
001034425 7001_ $$0P:(DE-HGF)0$$aCavasso, Domenico$$b4
001034425 7001_ $$0P:(DE-Juel1)158075$$aKoutsioumpas, Alexandros$$b5
001034425 7001_ $$0P:(DE-HGF)0$$aVarcamonti, Mario$$b6
001034425 7001_ $$0P:(DE-HGF)0$$aZanfardino, Anna$$b7
001034425 7001_ $$0P:(DE-HGF)0$$aFragneto, Giovanna$$b8
001034425 7001_ $$0P:(DE-HGF)0$$aPaduano, Luigi$$b9$$eCorresponding author
001034425 773__ $$0PERI:(DE-600)1491496-7$$a10.1016/j.molliq.2024.126086$$gVol. 414, p. 126086 -$$nPart A$$p126086 -$$tJournal of molecular liquids$$v414$$x0167-7322$$y2024
001034425 8564_ $$uhttps://juser.fz-juelich.de/record/1034425/files/DRAFT_LipidMembranes_EFV12Peptide_110724_RevisedVersion.pdf$$yPublished on 2024-09-23. Available in OpenAccess from 2026-09-23.
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001034425 9141_ $$y2024
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