ISIS Neutron and Muon Source Data Journal

Structural Implications of Novel Serine-rich Antimicrobial Peptides Killing Bacteria

Abstract: Modifying antimicrobial peptides' (AMPs) relative charges and hydrophobicity impacts their self-assembly and interaction with bacterial membranes. We produced novel, rationally designed AMPs utilising amino acids to selectively replace some lysine residues in the widely studied G(IIKK)3I-NH2 (G3) [1]. Using OFFSPEC, we have almost wholly unravelled how replacing lysine residues with serine influences peptide mechanism of action when binding to a model bacterial outer membrane mimic. Neutron reflection reveals serine homologues interact with the bacterial membrane differently depending on serine content, causing either the formation of lipid-peptide nano aggregates on the membrane surface or via direct lipid dissolving and membrane thinning. However, to fully deconstruct the entire interaction, we need to conduct further measurements with a fully deuterated bilayer system, uncovering the peptides' entire mechanism of action.

Principal Investigator: Miss Anna Stephens
Experimenter: Miss Tianhao Ge
Experimenter: Professor Jian Lu
Local Contact: Dr Luke Clifton

DOI: 10.5286/ISIS.E/ISIS.E.RB2400035

ISIS Experiment Number: RB2400035

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:
Miss Anna Stephens et al; (2024): Structural Implications of Novel Serine-rich Antimicrobial Peptides Killing Bacteria, STFC ISIS Neutron and Muon Source, https://doi.org/10.5286/ISIS.E/ISIS.E.RB2400035

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