{
  "annotation_id": "297da202-1504-49d0-9b0a-dffb21670852",
  "date_created": "2026-03-02T18:01:32.279000Z",
  "date_modified": "2026-03-02T18:01:32.279000Z",
  "file_hash": "ca9d91591af46dd8023d114531ab2e9d125c42060678531fc4f5df76a2fd0e44",
  "private": false,
  "record": {
    "abstract": "Being HIV-1-PR an essential enzyme in the viral life cycle, its inhibition\ncan control AIDS. Because the folding of single domain proteins, like HIV-1-PR\nis controlled by local elementary structures (LES, folding units stabilized by\nstrongly interacting, highly conserved amino acids) which have evolved over\nmyriads of generations to recognize and strongly attract each other so as to\nmake the protein fold fast, we suggest a novel type of HIV-1-PR inhibitors\nwhich interfere with the folding of the protein: short peptides displaying the\nsame amino acid sequence of that of LES. Theoretical and experimental evidence\nfor the specificity and efficiency of such inhibitors are presented.",
    "arxiv_id": "q-bio/0408013",
    "authors": [
      "R. A. Broglia",
      "G. Tiana",
      "D. Provasi",
      "F. Simona",
      "L. Sutto",
      "F. Vasile",
      "M. Zanotti"
    ],
    "categories": [
      "q-bio.BM"
    ],
    "title": "Design of a folding inhibitor of the HIV-1 Protease",
    "url": "https://arxiv.org/abs/q-bio/0408013"
  },
  "schema_id": "dorsal/arxiv",
  "source": {
    "execution_id": "81f48625-cf17-4413-9bd5-9b8d54609ea4",
    "id": "arXiv Dataset IDs",
    "type": "Model",
    "variant": "snapshot-2026-03-01",
    "version": "0.1.0"
  },
  "user_id": 1000002
}