{
  "abstract": "Bioanalysis of the immune checkpoint inhibitor nivolumab is crucial for pharmacokinetic studies. However, conventional ligand-binding assays (LBAs) often suffer from the lot-to-lot variability of capture antibodies. Here, we developed a high-affinity anti-nivolumab DNA aptamer as a robust alternative reagent. An integrated strategy combining Fast Protein Liquid Chromatography-based screening, next-generation sequencing, aptamer search algorithm, and computational modeling enabled rapid aptamer identification and optimization. The anti-nivolumab aptamer, mutant 2-3, discovered through in silico modification exhibited a dissociation constant (KD) of 33 nM. Using this aptamer, an enzyme-linked aptamer assay (ELAA) successfully quantified nivolumab in 400-fold diluted plasma samples over a range of 0.02–5.0 µg/mL, demonstrating good precision with a coefficient of variation less than 11.9%. This novel analytical method provides a sufficient quantitative range for the bioanalysis of nivolumab, thus offering a robust, specific, and cost-effective alternative for future pharmacokinetic studies.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 11,
  "authors": [
    {
      "name": "Taisei Hojo"
    },
    {
      "name": "Nao Kobayashi"
    },
    {
      "name": "Chiho Hirayama"
    },
    {
      "name": "Jiaxing Tong"
    },
    {
      "name": "Naruma Uchidate"
    },
    {
      "name": "Aogu Furusho"
    },
    {
      "name": "Kenji Kojima"
    },
    {
      "name": "Eiji Sugiyama"
    },
    {
      "name": "Hajime Mizuno"
    },
    {
      "name": "Hideki Hayashi"
    },
    {
      "name": "Kenichiro Todoroki"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/frjtb02t8zb69.bib",
  "cited_by": 0,
  "doi": "10.1248/cpb.c25-00788",
  "fulltext_url": "https://www.jstage.jst.go.jp/article/cpb/74/8/74_c25-00788/_article",
  "id": "frjtb02t8zb69",
  "issns": [
    "1347-5223",
    "0009-2363"
  ],
  "landing_url": "https://www.jstage.jst.go.jp/article/cpb/74/8/74_c25-00788/_article",
  "language": null,
  "licence": "CC-BY-NC",
  "licence_label": "CC BY-NC",
  "licence_source": "journal",
  "licence_url": "https://creativecommons.org/licenses/by-nc/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "jstage-journal",
      "chemistry/medicinal"
    ],
    [
      "openalex",
      "1312|Advanced biosensing and bioanalysis techniques"
    ]
  ],
  "openalex": "W7171996503",
  "pdf_url": "https://www.jstage.jst.go.jp/article/cpb/74/8/74_c25-00788/_pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-08-01",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/frjtb02t8zb69.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:34Z",
      "native_id": "10.1248/cpb.c25-00788",
      "source": "jstage",
      "url": "https://www.jstage.jst.go.jp/article/cpb/74/8/74_c25-00788/_article"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|Advanced biosensing and bioanalysis techniques",
      "subfield": "molecular-biology"
    }
  ],
  "title": "High-Affinity Anti-nivolumab DNA Aptamer: A Novel Capture Reagent for Its Bioanalysis by an Enzyme-Linked Aptamer Assay",
  "title_text": "High-Affinity Anti-nivolumab DNA Aptamer: A Novel Capture Reagent for Its Bioanalysis by an Enzyme-Linked Aptamer Assay",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:17:34Z",
  "url": "https://research.draconitic.com/paper/frjtb02t8zb69",
  "venue": "Chemical and Pharmaceutical Bulletin",
  "versions": []
}