DOI > 10.5291/ILL-DATA.8-02-769

This proposal is publicly available since 12/08/2021

Title

Probing cardiolipin layer structure on tuned surfaces with Neutron Reflectometry for the inclusion of ion transporting membrane proteins

Abstract

We propose Neutron Reflectometry (NR) experiments in order to characterize at the nanoscale the structure of pure cardiolipin deposits onto flat substrates of controlled interfacial properties. Although cardiolipin is an important lipid from the mitochondrial membrane, it has seldom been characterized in its pure form. We will investigate the effect of both cardiolipin surface concentration and of the substrate interfacial properties (hydrophilicity and surface charges). These properties are easily tuned by the grafting of functional groups onto the substrates by surface chemistry or electrochemistry. We will further investigate the incorporation of the membrane transport protein NhaA, a sodium-proton antiporter into the characterized cardiolipin bilayer. The NhaA function is to specifically transport ions across a membrane to create a voltage from which energy can be recovered. This research is relevant to the design of efficient and stable biomimetic membranes for sustainable fuel cells relying on salt gradients and will be carried out within the funded collaborative project ANR bioWATTS (ANR-15-CE05-0003-01, 2016-19) between UMR CNRS 5525 (Grenoble) and 6226 (Rennes).

Experimental Report

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Data Citation

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

MACCARINI Marco; ALCARAZ Jean Pierre; BARRIERE Frederic; FLINOIS Thomas; FRAGNETO Giovanna; Estelle Lebègue and MARTIN Donald. (2016). Probing cardiolipin layer structure on tuned surfaces with Neutron Reflectometry for the inclusion of ion transporting membrane proteins. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-02-769

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Metadata

Experiment Parameters

  • Environment temperature

    10-50 C
  • Experiment moment

    0.006 - 0.25 inv A

Sample Parameters

  • Formula

    • Membrane Protein
    • Cardiolipin