{
  "annotation_id": "d0bb5295-6a06-447b-a6a2-7432c9569714",
  "date_created": "2026-03-02T18:01:32.336000Z",
  "date_modified": "2026-03-02T18:01:32.336000Z",
  "file_hash": "01c0a1c7452c2bbd26c46eb366aa706b6da8aaaa1bfdcb110d60c0803d820b6b",
  "private": false,
  "record": {
    "abstract": "The 16-22 amino acid fragment of the beta-amyloid peptide associated with the\nAlzheimer\u0027s disease, Abeta, is capable of forming amyloid fibrils. Here we\nstudy the aggregation mechanism of Abeta(16-22) peptides by unbiased\nthermodynamic simulations at the atomic level for systems of one, three and six\nAbeta(16-22) peptides. We find that the isolated Abeta(16-22) peptide is mainly\na random coil in the sense that both the alpha-helix and beta-strand contents\nare low, whereas the three- and six-chain systems form aggregated structures\nwith a high beta-sheet content. Furthermore, in agreement with experiments on\nAbeta(16-22) fibrils, we find that large parallel beta-sheets are unlikely to\nform. For the six-chain system, the aggregated structures can have many\ndifferent shapes, but certain particularly stable shapes can be identified.",
    "arxiv_id": "q-bio/0409005",
    "authors": [
      "Giorgio Favrin",
      "Anders Irb\u00e4ck",
      "Sandipan Mohanty"
    ],
    "categories": [
      "q-bio.BM"
    ],
    "doi": "10.1529/biophysj.104.046839",
    "journal_ref": "Biophys. J. 87 (2004) 3657-3664",
    "title": "Oligomerization of amyloid Abeta peptides using hydrogen bonds and   hydrophobicity forces",
    "url": "https://arxiv.org/abs/q-bio/0409005"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "8df2ce18-2dc1-401e-8217-d1052a676582",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}