{
  "abstract": "TSPO is a ubiquitous transmembrane protein used as a pharmacological marker in neuroimaging. The only known atomic structure of mammalian TSPOs comes from the solution NMR of mouse TSPO (mTSPO) bound to the PK11195 ligand and in a DPC surfactant environment. No structure is available in a biomimetic environment and without PK11195 which strongly stiffens the protein. We measured the effect of different amphiphilic environments on ligand-free mTSPO to study its structure/function and find optimal solubilization conditions. By replacing the SDS surfactant, where the recombinant protein is purified, with mixed lipid:surfactant (DMPC:DPC) micelles at different ratios (0:1, 1:2 and 2:1, w:w), the α-helix content and interactions and the intrinsic tryptophan (Trp) fluorescence of mTSPO are gradually increased. Small-angle X-ray scattering (SAXS) shows a more extended mTSPO/belt complex with the addition of lipids: Dmax ∼95 Å in DPC alone versus ∼142 Å in DMPC:DPC (1:2). SEC-MALLS shows that the molecular composition of the mTSPO belt is ∼98 molecules for DPC alone and ∼58 DMPC and ∼175 DPC for DMPC:DPC (1:2). Additionally, DMPC:DPC micelles stabilize mTSPO compared to DPC alone, where the protein has a greater propensity to aggregate. These structural changes are consistent with the increased affinity of mTSPO for the PK11195 ligand in presence of lipids (Kd ∼70 μM in DPC alone versus ∼0.91 μM in DMPC:DPC, 1:2), as measured by microscale thermophoresis (MST). In conclusion, mixed lipid:surfactant micelles open new possibilities for the stabilization of membrane proteins and for their study in solution in a more biomimetic amphiphilic environment.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 9,
  "authors": [
    {
      "name": "Christelle Saade"
    },
    {
      "name": "Alexandre Pozza"
    },
    {
      "name": "Françoise Bonneté"
    },
    {
      "name": "Stéphanie Finet"
    },
    {
      "name": "Viviane Lutz-Bueno"
    },
    {
      "name": "Mark Tully"
    },
    {
      "name": "Paloma Varela"
    },
    {
      "name": "Jean-Jacques Lacapère"
    },
    {
      "name": "Sophie Combet"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/3efchtrr1xr23.bib",
  "cited_by": 5,
  "doi": "10.1016/j.biochi.2024.04.008",
  "fulltext_url": null,
  "id": "3efchtrr1xr23",
  "issns": [
    "0300-9084",
    "1638-6183"
  ],
  "landing_url": "https://hal.science/hal-05768136v1",
  "language": "en",
  "licence": "CC-BY",
  "licence_label": "CC BY",
  "licence_source": "journal",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "hal",
      "0.sdv"
    ],
    [
      "openalex",
      "1312|Lipid Membrane Structure and Behavior"
    ]
  ],
  "openalex": "W4395052150",
  "pdf_url": "https://ars.els-cdn.com/content/image/1-s2.0-S030090842400083X-ga1_lrg.jpg",
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-28",
  "publisher": "Elsevier",
  "ris": "https://research.draconitic.com/paper/3efchtrr1xr23.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:42Z",
      "native_id": "hal-05768136",
      "source": "hal",
      "url": "https://hal.science/hal-05768136v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|Lipid Membrane Structure and Behavior",
      "subfield": "molecular-biology"
    }
  ],
  "title": "Enhanced structure/function of mTSPO translocator in lipid:surfactant mixed micelles",
  "title_text": "Enhanced structure/function of mTSPO translocator in lipid:surfactant mixed micelles",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:17:42Z",
  "url": "https://research.draconitic.com/paper/3efchtrr1xr23",
  "venue": "Biochimie",
  "versions": []
}