{
  "id": 12953081,
  "title": "Reply to: Structural polymorphism of amyloid fibrils in ATTR amyloidosis revealed by cryo-electron microscopy",
  "url": "https://urgent.news/2026/10/08/reply-to-structural-polymorphism-of-amyloid-fibrils-in-attr",
  "topic": "science",
  "section": "Science",
  "published": "2026-10-08T00:00:00.000Z",
  "source": {
    "name": "bioRxiv",
    "slug": "biorxiv",
    "url": "https://www.biorxiv.org/content/10.64898/2026.10.01.755719v1?rss=1"
  },
  "original_language": "en",
  "account": "A recent study published in Nature Communications in 2024 by Nguyen et al. reveals structural polymorphism in fibrils associated with ATTR amyloidosis. ATTR amyloidosis is characterized by the deposition of transthyretin amyloid fibrils in multiple organs, leading to significant variations in symptoms and outcomes. While previous research has suggested that differences in fibril structure may contribute to these phenotypic variations, past studies have primarily focused on ATTR amyloid diseases such as AA amyloidosis, tauopathies, and synucleinopathies.\n\nIn the case of ATTR amyloidosis, most fibrils share a similar fold across patients and affected organs. However, a notable exception was reported in a study by Nguyen et al., which identified two co-existing polymorphs in cardiac fibrils from three patients with the ATTRv-I84S variant. These polymorphs differ in the conformation of the segment Gly57 to Gly67, known as the gate. One polymorph exhibits an open conformation, exposing a central polar channel within the fibril core, while the other maintains a closed conformation, shielding the channel.\n\nThe implications of these polymorphs extend beyond cardiac tissue, but this remains uncertain. The current study aims to address this question by expanding the analysis to additional organs from a fourth patient with ATTRv-I84S amyloidosis.",
  "summary": "In the paper by Nguyen et al, published in Nature Communications in 2024, we describe structural polymorphism in fibrils extracted from patients with ATTR amyloidosis. ATTR amyloidosis is characterized by deposition of transthyretin amyloid fibrils across multiple organs, resulting in marked phenotypic variability. Previous studies on ATTR suggest its phenotypic variability may be linked to…",
  "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."
}