DOI > 10.5291/ILL-DATA.8-02-869

This proposal is publicly available since 09/16/2024

Title

Dynamics of E. coli membrane mimics: influence of antimicrobial peptides on the flip-flop rate

Abstract

In this work we aim to further explore how antimicrobial peptides with different structures, incl. alphahelical, random coiled, beta sheets, affect the dynamics of model membrane systems mimicking E- coli using Time resolved SANS and contrast variation. The structural characterization and interactions with membranes have already been carried out using SAXS. By comparing the structural data and TR-SANS, we hope to clarify whether increased flip-flop is a common feature of such peptides and ultimately, conclude about the possible role in the mode of action of AMPs. Increased flip-flop is believed to be linked to increased ion transport through the membrane, causing disturbed osmotic regulation and cell death. The use of neutrons is crucial to be able to explore these systems as no other methods is able to probe both exchange and flip-flop kinetics without significant physical/chemical perturbation.

Experimental Report

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Data Citation

The recommended format for citing this dataset in a research publication is in the following format:

NIELSEN Josefine Eilsoe; CARDENAS; håvard jenssen; LONE Abdullah; LUND Reidar; MOLCHANOVA Natalia and PREVOST Sylvain. (2019). Dynamics of E. coli membrane mimics: influence of antimicrobial peptides on the flip-flop rate. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-02-869

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Metadata

Experiment Parameters

  • Environment temperature

    27-57 C
  • Experiment energy

    0.001-0.5Å
  • Experiment res energy

    10%

Sample Parameters

  • Formula

    • 1,2-dimyristoyl-sn-glycero-3-phosphoethanolamine
    • 1,2-dimyristoyl-sn-glycero-3-[phospho-rac-(1-glycerol)] (sodium salt)
    • C77H132N18O20 (peptide)
    • 1,2-dimyristoyl-d54-sn-glycero-3-[phospho-rac-(1-glycerol)] (sodium salt)
    • 1,2-dimyristoyl-d54-sn-glycero-3-phosphoethanolamine
    • C106H140ClN33O14 (peptide)