ISIS Neutron and Muon Source Data Journal

Interaction of an antimicrobial peptide from Lactobacillus gasseri supernatant with lipid bilayers mimicking the bacterial outer membrane

Abstract: A short peptide, composed of 12 amino acids (EFVFVAHAVPVM), presenting a strongly hydrophobic character, was recently isolated from Lactobacillus gasseri supernatant (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. AMP12 was also hypothesized to penetrate into the cell given its small size and its character strongly hydrophobic. We are interested in the characterization of the interaction between AMP12 and lipid bilayers as mimics of the bacterial membrane. NR measurements can provide unique information on the mechanism of action of AMP12. We propose to characterize asymmetric lipid bilayers containing LPS from Escherichia Coli to investigate the location of AMP12 with respect to the bilayer.

Principal Investigator: Dr Giuseppe Vitiello
Local Contact: Dr Maxmilian Skoda
Experimenter: Professor Luigi Paduano
Experimenter: Mr Romualdo Troisi
Local Contact: Dr John Webster

DOI: 10.5286/ISIS.E.RB1920349

ISIS Experiment Number: RB1920349

Publisher: STFC ISIS Neutron and Muon Source

Data format: RAW/Nexus
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Data Citation

The recommended format for citing this dataset in a research publication is as:
[author], [date], [title], [publisher], [doi]

For Example:
Dr Giuseppe Vitiello et al; (2020): Interaction of an antimicrobial peptide from Lactobacillus gasseri supernatant with lipid bilayers mimicking the bacterial outer membrane, STFC ISIS Neutron and Muon Source, https://doi.org/10.5286/ISIS.E.RB1920349

Data is released under the CC-BY-4.0 license.