{
  "abstract": "Neuropilin-1 (NRP-1) is associated with glioblastoma progression and contains a b1-domain pocket that binds the C-terminal region of VEGF-A165. Whether laminin-derived peptide fragments can associate with this site is unknown. AlphaFold 3 complex prediction followed by 15 s of all-atom production molecular dynamics simulation, trajectory-based pocket occupancy and interaction analyses, and FoldX energetic scoring was performed to compare binding of the laminin-derived pentapeptide Ac-Tyr-Ile-Gly-Ser-Arg-NH2 (peptide 1) with its retro (Ac-Arg-Ser-Gly-Ile-Tyr-NH2, peptide 2) and retro-inverso (Ac-arg-ser-Gly-ile-tyr-NH2, peptide 3) analogs. Peptide 1 showed the highest mean equilibrated occupancy of the canonical VEGF-A165 pocket (60.3 +/- 34.6%) compared with peptide 2 (25.9 +/- 32.7%) and peptide 3 (21.4 +/- 29.5%), while sampling interactions with canonical pocket residues including Asp320, Tyr297, and Tyr353; FoldX binding-energy estimates were similar across peptides despite their differing pocket persistence. Complementary nanoDSF measurements using recombinant NRP-1 and synthetic peptides yielded apparent dissociation constants in the low micromolar range for all three peptides (12.7 M - 33.3 M), providing experimental support for the predicted interactions. These results support persistent, sequence-dependent association of peptide 1 with the VEGF-A165 binding site of b1-NRP-1 and identify peptide analogs as a candidate for further optimization as an NRP-1-binding peptide.",
  "abstract_shown": true,
  "affiliations": [
    "Creighton University"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 2,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "E. Veltri"
    },
    {
      "name": "S. Lovas"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/cjbqxhhyz0yg4.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.10.27.762289",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.10.27.762289v1.full",
  "id": "cjbqxhhyz0yg4",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.10.27.762289v1",
  "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",
      "biophysics"
    ]
  ],
  "openalex": null,
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.10.27.762289v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-27",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/cjbqxhhyz0yg4.ris",
  "sources": [
    {
      "first_seen": "2026-10-31T00:21:20Z",
      "native_id": "10.64898/2026.10.27.762289",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.10.27.762289v2"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "biorxiv:biophysics",
      "subfield": "biophysics"
    }
  ],
  "title": "Laminin-Derived Peptides Bind Neuropilin-1 at the VEGF-A165 Binding Pocket",
  "title_text": "Laminin-Derived Peptides Bind Neuropilin-1 at the VEGF-A165 Binding Pocket",
  "type": "preprint",
  "updated_at": "2026-11-03T00:20:25Z",
  "url": "https://research.draconitic.com/paper/cjbqxhhyz0yg4",
  "venue": "bioRxiv",
  "versions": []
}