{
  "abstract": "Amyloid fibrils are protein aggregates associated with neurodegenerative diseases. Their formation proceeds through protein- and condition-dependent microscopic pathways that can generate structurally and biologically distinct aggregates, yet these pathways are inferred from ensemble-averaged measurements. Amyloid formation is often slow under quiescent conditions, prompting agitation. However, conventional agitation precludes simultaneous high-resolution solution nuclear magnetic resonance (NMR) spectroscopy, limiting site-specific kinetic analysis of microscopic aggregation pathways. Here we present an integrated Rheo-NMR platform combining controlled shear flow, time-resolved NMR spectroscopy and mechanistic kinetic modeling to quantify site-specific amyloid-formation kinetics in a single, continuously monitored reaction. Applied to -synuclein under dilute and polyethylene glycol (PEG)-induced liquid-liquid phase separation (LLPS) conditions, the method revealed environment-dependent redistribution of kinetic signatures associated with primary nucleation-elongation and secondary nucleation-elongation pathways across the sequence. The platform distinguishes changes in overall aggregation rates from differences in residue-specific kinetic profiles, providing a quantitative framework for dissecting environment-dependent amyloid formation.",
  "abstract_shown": true,
  "affiliations": [
    "Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 8,
  "authors": [
    {
      "name": "M. So"
    },
    {
      "name": "K. Sato"
    },
    {
      "name": "K. Yoshioka"
    },
    {
      "name": "Y. Shimada"
    },
    {
      "name": "D. Morimoto"
    },
    {
      "name": "H. Nakamura"
    },
    {
      "name": "A. Furukawa"
    },
    {
      "affs": [
        0
      ],
      "name": "K. Sugase"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/5e5jy5d2h402f.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.10.19.760037",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.10.19.760037v1.full",
  "id": "5e5jy5d2h402f",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.10.19.760037v1",
  "language": null,
  "licence": "CC-BY",
  "licence_label": "CC BY",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "biorxiv",
      "biochemistry"
    ],
    [
      "openalex",
      "2737|Alzheimer's disease research and treatments"
    ]
  ],
  "openalex": "W7223008630",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.10.19.760037v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-19",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/5e5jy5d2h402f.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:28:46Z",
      "native_id": "10.64898/2026.10.19.760037",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.10.19.760037v1"
    }
  ],
  "subjects": [
    {
      "field": "medicine",
      "origin": "openalex:2737|Alzheimer's disease research and treatments",
      "subfield": "physiology"
    }
  ],
  "title": "An integrated Rheo-NMR platform for real-time, site-specific kinetic analysis of amyloid formation",
  "title_text": "An integrated Rheo-NMR platform for real-time, site-specific kinetic analysis of amyloid formation",
  "type": "preprint",
  "updated_at": "2026-10-30T12:28:46Z",
  "url": "https://research.draconitic.com/paper/5e5jy5d2h402f",
  "venue": "bioRxiv",
  "versions": []
}