{
  "abstract": "Identifying short peptides that bind therapeutically relevant proteins is a practical step toward developing peptide-based inhibitors. Here we screened 64 tetrapeptides for binding to the IL-17A homodimer using classical all-atom molecular dynamics simulations (GROMACS 2022.2, FF19SB force field, TIP3P water, 200 ns production per complex). Binding was ranked by a composite score that combines short-range interaction energies (Coul-SR + LJ-SR), close-contact frequency, mean intermolecular distance, and hydrogen bond occupancy. The tetrapeptide LYS-THR-CYS-ASP achieved the highest score in the set (composite score 2.85, total interaction energy -556 kJ/mol, average 8.0 H-bonds). Across all 64 simulations, electrostatic interactions accounted for approximately 72% of the total interaction energy. Stronger binders tended to contain charged and polar residues (Asp, Glu, Cys, Arg, Thr), while weaker binders were enriched in hydrophobic residues. Contact analysis identified a recurring interaction surface on IL-17A centered on cysteine and aromatic residues (Chain A: CYS87, Chain B:CYS196, A:HIS86, B:TYR175, B:HIS195), which we describe as a cysteine-aromatic cradle. These results nominate LYS-THR-CYS-ASP as a candidate for experimental binding validation and suggest simple sequence guidelines for designing IL-17A-targeting peptides.",
  "abstract_shown": true,
  "affiliations": [
    "ShenZhen UnibindMD Computation Biotech Co., Ltd."
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 2,
  "authors": [
    {
      "name": "W. Xu"
    },
    {
      "affs": [
        0
      ],
      "name": "W. Fu"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/21x0ea021je9s.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.09.04.749315",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.09.04.749315v1.full",
  "id": "21x0ea021je9s",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.09.04.749315v1",
  "language": null,
  "licence": "CC-BY",
  "licence_label": "CC BY",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "biorxiv",
      "biochemistry"
    ],
    [
      "openalex",
      "1312|Protein Structure and Dynamics"
    ]
  ],
  "openalex": "W7211889075",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.09.04.749315v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-04",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/21x0ea021je9s.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:19:55Z",
      "native_id": "10.64898/2026.09.04.749315",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.09.04.749315v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|Protein Structure and Dynamics",
      "subfield": "molecular-biology"
    }
  ],
  "title": "Screening Peptide Binders to IL-17A Using Classical Molecular Dynamics",
  "title_text": "Screening Peptide Binders to IL-17A Using Classical Molecular Dynamics",
  "type": "preprint",
  "updated_at": "2026-10-30T12:19:55Z",
  "url": "https://research.draconitic.com/paper/21x0ea021je9s",
  "venue": "bioRxiv",
  "versions": []
}