Impact of an antimicrobial peptide from Lactobacillus gasseri supernatant on the structure of lipid bilayer mimicking the bacterial inner me
Antimicrobial peptides (AMPs) are promising candidates as future therapeutics against the antibiotic resistance caused by pathogenic bacteria. Most known AMPs are small peptides, formed of 12 to 60 amino acids with molecular masses < 10 kDa. Recently, several AMPs have been identified in the marine environment, which act as the first line of defense against a broad spectrum of pathogens. A short peptide, composed of 12 amino acids (EFVFVAHAVPVM) with a molecular weight of 1333 Da, and presenting a strongly hydrophobic character, was recently isolated from Lactobacillus gasseri supernatant (named hereafter AMP12). This peptide has shown antimicrobial activity and may also bind the TLR4 receptor or lipopolysaccharides (LPS), which can result in blocking the activation of the inflammatory pathway. We are interested in the characterization of the interaction between AMP12 and lipid bilayers and NR can provide unique information on the action mechanism of AMP12. We propose to characterize lipid bilayers containing LPS from Escherichia Coli as mimics of the bacterial membrane and to investigate the location of AMP12 with respect to the bilayer.
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VITIELLO Giuseppe; FRAGNETO Giovanna; LUCHINI Alessandra; PADUANO Luigi and RUSSO KRAUSS Irene. (2018). Impact of an antimicrobial peptide from Lactobacillus gasseri supernatant on the structure of lipid bilayer mimicking the bacterial inner me. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-02-826
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