{
  "abstract": "The LRRK2 kinase has emerged as a priority therapeutic target due to its welldocumented role in Parkinson-s diseases (PD). One of LRRK2's key partners is the phosphatase PP1, which dephosphorylates LRRK2. Therefore, modulating this protein/protein interaction represents a promising therapeutic strategy for PD. We have developed a bi-functional peptide, PEP 3, capable of crossing the blood-brain barrier (BBB) and disrupting the LRRK2/PP1 interaction. In vitro competition assays confirmed that PEP 3 specifically targets this interaction. The in vivo imaging demonstrated that the peptide remains detectable in the mouse brain up to 6 hours or retro-orbital vein post-injection. The PEP 3 peptide does not show chronic toxicity in CD1 mice and is resistant to degradation by mouse, human, dog and monkey serum proteases. In mouse models overexpressing alpha-synuclein, repeated intraperitoneal injections of PEP 3 for 15 and 30 days were well tolerated. Immunohistochemistry revealed a significant reduction of dopaminergic cell death in the substantia nigra, and quantification of phosphorylated pathological alpha-synuclein showed decreased levels in the PEP 3-treated group compared to controls. These findings support the potential of PEP 3 as a therapeutic agent for Parkinson's disease.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 11,
  "authors": [
    {
      "name": "Severine Loisel"
    },
    {
      "name": "Fanny Petit"
    },
    {
      "name": "Gwenaelle Auregan"
    },
    {
      "name": "Martine Guillermier"
    },
    {
      "name": "Marjorie Benfissa"
    },
    {
      "name": "Pauline Gipchtein"
    },
    {
      "name": "Asma Touffeil Mohamed"
    },
    {
      "name": "Kristina Posnograjeva"
    },
    {
      "name": "Tambet Teesalu"
    },
    {
      "name": "Romina Aron Badin"
    },
    {
      "name": "Angelita Rebollo"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/1gb7jznpetcmf.bib",
  "cited_by": 0,
  "doi": "10.4236/apd.2026.153003",
  "fulltext_url": null,
  "id": "1gb7jznpetcmf",
  "issns": [
    "2169-9712",
    "2169-9720"
  ],
  "landing_url": "https://cnrs.hal.science/hal-05798064v1",
  "language": "en",
  "licence": "CC-BY-4.0",
  "licence_label": "CC BY 4.0",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "hal",
      "0.sdv"
    ],
    [
      "openalex",
      "2728|Parkinson's Disease Mechanisms and Treatments"
    ]
  ],
  "openalex": "W7213967721",
  "pdf_url": "https://cnrs.hal.science/hal-05798064/document",
  "pmcid": null,
  "pmid": null,
  "published": "2026-08-31",
  "publisher": "Scientific Research Publishing Inc.",
  "ris": "https://research.draconitic.com/paper/1gb7jznpetcmf.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:56Z",
      "native_id": "hal-05798064",
      "source": "hal",
      "url": "https://cnrs.hal.science/hal-05798064v1"
    }
  ],
  "subjects": [
    {
      "field": "medicine",
      "origin": "openalex:2728|Parkinson's Disease Mechanisms and Treatments",
      "subfield": "neurology"
    }
  ],
  "title": "Brain-Specific PP1/LRRK2 Interaction-Tageting Peptides as a Novel Strategy for Parkinson’s Disease Treatment",
  "title_text": "Brain-Specific PP1/LRRK2 Interaction-Tageting Peptides as a Novel Strategy for Parkinson’s Disease Treatment",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:17:56Z",
  "url": "https://research.draconitic.com/paper/1gb7jznpetcmf",
  "venue": "Advances in Parkinson's Disease",
  "versions": []
}