{
  "abstract": "Nanoplastic contamination is increasingly recognized as a biochemical stressor, yet the molecular determinants governing how polymer fragment size dictates protein-level interactions remain poorly understood. Here, we combine molecular docking and all-atom molecular dynamics simulations to characterize the interaction of polyethylene (PE) oligomers of increasing length (n = 3, 5, 7, and 14 repeat units) with human catalase, a tetrameric heme enzyme central to cellular antioxidant defense. Single-chain simulations reveal that short PE fragments (3-, 5-, and 7-mer) migrate from an initial domain-connector pose toward a heme-proximal, previously characterized inhibitor-binding site, whereas the 14-mer remains kinetically confined to a peripheral surface site, implicating short-chain PE as a potential catalase inhibitor. In multichain corona systems, backbone dynamics show a non-monotonic, chain-length-dependent destabilization, with the 3- and 5-mer inducing the greatest structural perturbation and the 14-mer best preserving native-like dynamics despite forming an extensive, percolating surface network across all four subunits. MM-PBSA free energy decomposition identifies van der Waals interactions as the dominant thermodynamic driver of binding, while electrostatic surface mapping indicates that cationic surface patches instead govern long-range spatial targeting of PE chains. These findings establish a framework linking nanoplastic fragment size to protein-level toxicity, with direct implications for assessing the biochemical risk of environmentally weathered polyethylene.",
  "abstract_shown": true,
  "affiliations": [
    "National Institute of Technology Warangal"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 2,
  "authors": [
    {
      "name": "S. Tanaya"
    },
    {
      "affs": [
        0
      ],
      "name": "S. L. Rath"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/7gdaknfvgc29z.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.10.08.757803",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.10.08.757803v1.full",
  "id": "7gdaknfvgc29z",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.10.08.757803v1",
  "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",
      "2310|Microplastics and Plastic Pollution"
    ]
  ],
  "openalex": "W7221478973",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.10.08.757803v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-08",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/7gdaknfvgc29z.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:27:02Z",
      "native_id": "10.64898/2026.10.08.757803",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.10.08.757803v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "biorxiv:biophysics",
      "subfield": "biophysics"
    }
  ],
  "title": "Chain-Length-Dependent Interactions of Polyethylene Nanoplastics with Human Catalase reveals Size based Nanoplastic Toxicity",
  "title_text": "Chain-Length-Dependent Interactions of Polyethylene Nanoplastics with Human Catalase reveals Size based Nanoplastic Toxicity",
  "type": "preprint",
  "updated_at": "2026-10-30T12:27:02Z",
  "url": "https://research.draconitic.com/paper/7gdaknfvgc29z",
  "venue": "bioRxiv",
  "versions": []
}