{
  "abstract": "Protein nanofibers are hold great promise as genetically programmable scaffolds for constructing functional material interfaces. AtaA, a giant trimeric autotransporter adhesin from Acinetobacter sp. Tol 5, forms an elongated architecture from the bacterial cell surface, enabling the cells to adhere directly to a wide variety of abiotic surfaces. However, the potential use of AtaA as a scaffold with additional biological functions remains largely unexplored. In this study, we investigated the use of AtaA as a self-immobilizing scaffold for constructing enzymatically active surfaces via horseradish peroxidase (HRP)-catalyzed tyrosine coupling. We prepared a recombinant AtaA nanofiber fragment (NhNs-AtaA) and its derivative containing two tyrosine-containing loop structures (YL-NhNs-AtaA). Both recombinant proteins retained their adhesive properties. Treatment with HRP and H2O2 generated high-molecular-weight products from both proteins, and dityrosine fluorescence emission indicated the formation of tyrosine-derived covalent cross-links. Y-Loop insertion further increased the consumption of monomeric AtaA and promoted the formation of high-molecular-weight products. The removal of arginine, which was included during purification, further increased the loss of monomeric AtaA in both constructs, indicating that intermolecular protein association influenced productive AtaA cross-linking. NhNs-AtaA and YL-NhNs-AtaA were combined with Y-tagged bacterial alkaline phosphatase (BAP-Y). HRP-mediated coupling generated high-molecular-weight products consistent with the cross-linked AtaA-BAP-Y conjugates and enabled the retention of BAP activity on AtaA-coated surfaces without prior chemical modification. Although Y-Loop insertion enhanced polymerization in solution, it reduced AtaA adhesion and consequently lowered surface-bound phosphatase activity, revealing a trade-off between cross-linking reactivity and native adhesive function. These findings establish AtaA as a self-immobilizing protein nanofiber scaffold for constructing enzymatically active surfaces, and suggest the potential extension of this strategy to other AtaA-based interfaces.",
  "abstract_shown": true,
  "affiliations": [
    "Nagahama Institute of Bio-Science and Technology"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 9,
  "authors": [
    {
      "name": "Y. Yokoe"
    },
    {
      "name": "S. Yoshimoto"
    },
    {
      "name": "K. Miniamihata"
    },
    {
      "name": "R. Sugimoto"
    },
    {
      "name": "A. Nagatani"
    },
    {
      "name": "A. Nara"
    },
    {
      "name": "N. Kamiya"
    },
    {
      "name": "K. Hori"
    },
    {
      "affs": [
        0
      ],
      "name": "M. Ishikawa"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/592bf63a8rwmd.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.09.30.755837",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.09.30.755837v1.full",
  "id": "592bf63a8rwmd",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.09.30.755837v1",
  "language": null,
  "licence": "CC-BY-NC-ND",
  "licence_label": "CC BY-NC-ND",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by-nc-nd/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "biorxiv",
      "bioengineering"
    ],
    [
      "openalex",
      "1312|Biochemical and Structural Characterization"
    ]
  ],
  "openalex": "W7215962790",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.09.30.755837v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-30",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/592bf63a8rwmd.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:25:51Z",
      "native_id": "10.64898/2026.09.30.755837",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.09.30.755837v2"
    }
  ],
  "subjects": [
    {
      "field": "biology",
      "origin": "biorxiv:bioengineering",
      "subfield": "systems-synthetic"
    }
  ],
  "title": "AtaA as a Self-Immobilizing Scaffold for Enzymatically Active Surfaces through Oxidative Tyrosine Coupling",
  "title_text": "AtaA as a Self-Immobilizing Scaffold for Enzymatically Active Surfaces through Oxidative Tyrosine Coupling",
  "type": "preprint",
  "updated_at": "2026-10-30T12:25:57Z",
  "url": "https://research.draconitic.com/paper/592bf63a8rwmd",
  "venue": "bioRxiv",
  "versions": []
}