{
  "abstract": "The actin cytoskeleton is a self-assembled material that acts as the mechanical scaffold of the cell. Within the cell, protein cross-linkers organize actin filaments into assemblies with various microstructures that support distinct physiological functions. These protein cross-linkers differ in structural features. To decouple the role of individual cross-linker properties in actin assembly microstructure and mechanics, we synthesize programmable cross-linkers using a DNA linker coupled to binding domains. We find that high affinity cross-linkers induce actin bundling, while low affinity cross-linkers form actin networks. Myosin II motors remodel and contract all cross-linked networks tested in distinct ways from uncross-linked networks. We find that networks with high affinity cross-linkers have different myosin induced dynamics than networks with low affinity cross-linkers. This research expands our understanding of how cells regulate their mechanics and microstructures, while also providing insight towards the structure-property relationship in complex soft materials.",
  "abstract_shown": true,
  "affiliations": [
    "Clemson University"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 4,
  "authors": [
    {
      "name": "C. A. Feigeles"
    },
    {
      "name": "M. Janquart"
    },
    {
      "name": "V. Armstrong"
    },
    {
      "affs": [
        0
      ],
      "name": "K. L. Weirich"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/fy2cywhphvybg.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.10.02.756345",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.10.02.756345v1.full",
  "id": "fy2cywhphvybg",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.10.02.756345v1",
  "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",
      "biophysics"
    ],
    [
      "openalex",
      "1307|Cellular Mechanics and Interactions"
    ]
  ],
  "openalex": "W7221137550",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.10.02.756345v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-02",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/fy2cywhphvybg.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:26:45Z",
      "native_id": "10.64898/2026.10.02.756345",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.10.02.756345v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "biorxiv:biophysics",
      "subfield": "biophysics"
    }
  ],
  "title": "Cross-linker binding strength influences actin assembly microstructure and myosin II driven remodeling",
  "title_text": "Cross-linker binding strength influences actin assembly microstructure and myosin II driven remodeling",
  "type": "preprint",
  "updated_at": "2026-10-30T12:26:45Z",
  "url": "https://research.draconitic.com/paper/fy2cywhphvybg",
  "venue": "bioRxiv",
  "versions": []
}