{
  "abstract": "Protein biosensors are important analytical and diagnostic tools that convert molecular recognition into measurable activity. Most common two-component biosensors require two non-competing recognition domains, yet binding affinity and specificity alone do not reliably predict their compatibility with the rest of the biosensor. We report a modular platform that exploits monomeric streptavidin (mSA2) as a surrogate recognition domain, enabling rapid functional evaluation of candidate binders in the context of biosensor scaffold without requiring a second ligand-specific binding protein. We established a chromatography-free protocol for recovering functional mSA2-based biosensor components from Escherichia coli. Using biotinylated small molecules methotrexate and vitamin D3, as well as heart failure protein biomarkers galectin-3 and S100A7 we demonstrate ligand-dependent reporter biosensor activation. The developed platform provides a scalable approach for rapid binder evaluation and biosensor prototyping, streamlining biosensor development using binding domains generated by directed evolution or computational protein design.",
  "abstract_shown": true,
  "affiliations": [
    "Queensland University Of Technology"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 5,
  "authors": [
    {
      "name": "R. Mutschler"
    },
    {
      "name": "Z. Guo"
    },
    {
      "name": "M. M. Fiorito"
    },
    {
      "name": "K. Alexandrov"
    },
    {
      "affs": [
        0
      ],
      "name": "Z. Cui"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/877ahqrk8cyxs.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.11.03.763809",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.11.03.763809v1.full",
  "id": "877ahqrk8cyxs",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.11.03.763809v1",
  "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",
      "synthetic biology"
    ]
  ],
  "openalex": null,
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.11.03.763809v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-11-03",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/877ahqrk8cyxs.ris",
  "sources": [
    {
      "first_seen": "2026-11-05T00:21:58Z",
      "native_id": "10.64898/2026.11.03.763809",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.11.03.763809v1"
    }
  ],
  "subjects": [
    {
      "field": "biology",
      "origin": "biorxiv:synthetic biology",
      "subfield": "systems-synthetic"
    }
  ],
  "title": "Functional analysis of small-molecule and protein binding domains using monomeric streptavidin-based two-component biosensors",
  "title_text": "Functional analysis of small-molecule and protein binding domains using monomeric streptavidin-based two-component biosensors",
  "type": "preprint",
  "updated_at": "2026-11-06T00:21:42Z",
  "url": "https://research.draconitic.com/paper/877ahqrk8cyxs",
  "venue": "bioRxiv",
  "versions": []
}