TY  - JOUR
AU  - Vitiello, Giuseppe
AU  - Luchini, Alessandra
AU  - Di Napoli, Michela
AU  - Gallucci, Noemi
AU  - Cavasso, Domenico
AU  - Koutsioumpas, Alexandros
AU  - Varcamonti, Mario
AU  - Zanfardino, Anna
AU  - Fragneto, Giovanna
AU  - Paduano, Luigi
TI  - The affinity towards the hydrophobic region of biomimicking bacterial membranes drives the antimicrobial activity of EFV12 peptide from Lactobacillus gasseri gut microbiota
JO  - Journal of molecular liquids
VL  - 414
IS  - Part A
SN  - 0167-7322
CY  - New York, NY [u.a.]
PB  - Elsevier
M1  - FZJ-2024-07206
SP  - 126086 -
PY  - 2024
AB  - The 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.
LB  - PUB:(DE-HGF)16
DO  - DOI:10.1016/j.molliq.2024.126086
UR  - https://juser.fz-juelich.de/record/1034425
ER  -