{
  "id": 18301018,
  "title": "Platycodin D2 Targets Vimentin to Suppress Fibroblast-Myofibroblast Transition: A Novel Therapeutic Strategy Against Pulmonary Fibrosis",
  "url": "https://urgent.news/2026/11/05/platycodin-d2-targets-vimentin-to-suppress-fibroblast-myofibroblast",
  "topic": "culture",
  "section": "Culture",
  "published": "2026-11-05T00:00:00.000Z",
  "source": {
    "name": "bioRxiv",
    "slug": "biorxiv",
    "url": "https://www.biorxiv.org/content/10.64898/2026.11.03.763586v1?rss=1"
  },
  "original_language": "en",
  "account": "Pulmonary fibrosis, a debilitating lung disorder marked by excessive extracellular matrix accumulation and irreversible lung function decline, presents few therapeutic options. Fibroblast activation and fibrogenesis hinge on vimentin, a type III intermediate filament protein, offering a potential drug target. Researchers screened for vimentin ligands using virtual screening. Subsequent SPR assays confirmed the compound-binding affinity to vimentin. CETSA and CD spectroscopy were then employed to monitor structural alterations in proteins post-binding. In vitro FMT and in vivo bleomycin-induced pulmonary fibrosis models were utilized to evaluate antifibrotic efficacy. Mutagenesis assays were conducted to pinpoint pivotal binding amino acid residues.\n\nPlatycodin D2 (PD2), extracted from Platycodon grandiflorus, emerged as a promising novel high-affinity vimentin ligand with a dissociation constant of 392.8 nM. PD2 directly binds vimentin, modifies its secondary structure, and triggers insoluble aggregation. Its capacity to inhibit TGF-{beta}1-induced FMT in vitro and alleviate bleomycin-induced pulmonary fibrosis in vivo is noteworthy. Moreover, mutagenesis validation validated that crucial residues (Glu138 in chain A, Glu132 and Glu143 in chain B, along with Glu50 and Arg54 in chain C) are imperative for this interaction. In summary, PD2 has been identified as a groundbreaking pharmacological agent that induces aberrant vimentin aggregation, providing a unique target-driven approach for the development of antifibrotic drugs.",
  "summary": "Background Pulmonary fibrosis is a progressive lung disease characterized by excessive extracellular matrix deposition and irreversible decline in lung function with limited effective therapeutic targets. Vimentin, a type III intermediate filament protein, plays a critical role in fibroblast activation and fibrogenesis, representing a promising drug target. Methods Novel vimentin ligands were…",
  "key_points": [],
  "editors_take": null,
  "illustration": null,
  "coverage": {
    "outlets": 1,
    "also_reported_by": []
  },
  "ai_generated": true,
  "disclaimer": "Summaries, key points and the editor’s take are written by software from other outlets’ reporting and may contain errors — always check the linked original."
}