{
  "abstract": "Engineering the spatial organization of proteins offers a powerful strategy for controlling biochemical reactions and material properties in synthetic cells. However, dynamically organizing multiple proteins at the nanometer scale remains challenging. We developed asymmetric lipid–oleosin hybrid vesicles in which engineered oleosin molecules served as membrane-forming scaffolds with two orthogonal conjugation systems. External chemical stimuli rapidly recruited two distinct proteins to individual oleosin molecules, generating persistent nanometer-scale proximity, as demonstrated by single-molecule tracking. In an alditol oxidase–horseradish peroxidase cascade, organization of both enzymes on the same oleosin scaffold enhanced product formation compared with intermolecular membrane recruitment. This localized cascade further drove stimulus-responsive polymerization to form membrane-associated cytoskeleton-like structures, increasing vesicle resistance to hypertonic stress. This programmable membrane scaffold couples external signals with molecular organization, enhanced biochemical reactions, and membrane mechanics, providing a framework for engineering synthetic cells that convert chemical inputs into programmable reactions and material outputs.",
  "abstract_shown": true,
  "affiliations": [
    "Graduate School of Science and Technology",
    "Gunma University",
    "Division of Advanced Bioimaging",
    "National Cancer Center Research Institute"
  ],
  "article_type": null,
  "arxiv": null,
  "author_total": 3,
  "authors": [
    {
      "affs": [
        0,
        1
      ],
      "name": "Masato Suzuki"
    },
    {
      "affs": [
        2,
        3
      ],
      "name": "Rinshi S. Kasai"
    },
    {
      "affs": [
        0,
        1
      ],
      "name": "Koki Kamiya",
      "orcid": "0000-0001-9143-9841"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/c4z90jjeyf7a2.bib",
  "cited_by": 0,
  "doi": "10.26434/chemrxiv.15008603/v1",
  "fulltext_url": null,
  "id": "c4z90jjeyf7a2",
  "issns": [],
  "landing_url": "https://chemrxiv.org/doi/full/10.26434/chemrxiv.15008603/v1",
  "language": null,
  "licence": "CC-BY-NC-ND",
  "licence_label": "CC BY-NC-ND",
  "licence_source": "journal",
  "licence_url": "https://creativecommons.org/licenses/by-nc-nd/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "openalex",
      "1312|Lipid Membrane Structure and Behavior"
    ]
  ],
  "openalex": "W7212189057",
  "pdf_url": "https://chemrxiv.org/doi/pdf/10.26434/chemrxiv.15008603/v1",
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-09",
  "publisher": "American Chemical Society (ACS)",
  "ris": "https://research.draconitic.com/paper/c4z90jjeyf7a2.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:19Z",
      "native_id": "10.26434/chemrxiv.15008603",
      "source": "chemrxiv",
      "url": "https://chemrxiv.org/doi/full/10.26434/chemrxiv.15008603/v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|Lipid Membrane Structure and Behavior",
      "subfield": "molecular-biology"
    }
  ],
  "title": "Accumulation of enzymes on the lipid-oleosin membarnes",
  "title_text": "Accumulation of enzymes on the lipid-oleosin membarnes",
  "type": "preprint",
  "updated_at": "2026-10-30T12:17:19Z",
  "url": "https://research.draconitic.com/paper/c4z90jjeyf7a2",
  "venue": "ChemRxiv",
  "versions": []
}