{
  "abstract": "Glucagon-like peptide-1 (GLP-1) is best known as a receptor agonist, yet its peptide-level behavior in protein-rich environments remains poorly defined. Here, a GLP-1-directed photoaffinity probe recovered a predefined Aβ42 spike-in from cell lysates, while endogenous actin and α-synuclein were detected in the recovered fractions. This observation motivated chemically defined assembly studies with the actinlinked β-thymosin reference TMSB4Y. Thioflavin T (ThT) kinetics and endpoint electron microscopy (EM) revealed no single pro- or antiassembly response. GLP-1 advanced the ThT-positive transition of Tyr10-unmodified Aβ42, whereas TMSB4Y attenuated it. Phosphorylation or nitration at Tyr10 changed both the direction and timing of these effects, and GLP-1 added after assembly had begun redirected established trajectories in a Tyr10-modification-dependent manner. Ser18 O-GlcNAcylation of GLP-1 provided an orthogonal perturbation, suppressing the Tyr10-unmodified response while enhancing the nitrated trajectory and delaying the phosphorylated one. Together, capture in a complex protein background and assembly in defined mixtures identify GLP-1 as a context-sensitive modulator of Aβ42 assembly rather than a fixed promoter or inhibitor.",
  "abstract_shown": true,
  "affiliations": [
    "Institute of Chemistry",
    "Humboldt-Universität zu Berlin Brook-Taylor-Str. 2, 12489 Berlin"
  ],
  "article_type": null,
  "arxiv": null,
  "author_total": 1,
  "authors": [
    {
      "affs": [
        0,
        1
      ],
      "name": "Pritam Ghosh",
      "orcid": "0000-0002-2345-8036"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/6r9eh7dy3ej3f.bib",
  "cited_by": 0,
  "doi": "10.26434/chemrxiv.15010165/v1",
  "fulltext_url": null,
  "id": "6r9eh7dy3ej3f",
  "issns": [],
  "landing_url": "https://chemrxiv.org/doi/full/10.26434/chemrxiv.15010165/v1",
  "language": null,
  "licence": "CC-BY",
  "licence_label": "CC BY",
  "licence_source": "journal",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "openalex",
      "2737|Alzheimer's disease research and treatments"
    ]
  ],
  "openalex": "W7221148068",
  "pdf_url": "https://chemrxiv.org/doi/pdf/10.26434/chemrxiv.15010165/v1",
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-09",
  "publisher": "American Chemical Society (ACS)",
  "ris": "https://research.draconitic.com/paper/6r9eh7dy3ej3f.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:22Z",
      "native_id": "10.26434/chemrxiv.15010165",
      "source": "chemrxiv",
      "url": "https://chemrxiv.org/doi/full/10.26434/chemrxiv.15010165/v1"
    }
  ],
  "subjects": [
    {
      "field": "medicine",
      "origin": "openalex:2737|Alzheimer's disease research and treatments",
      "subfield": "physiology"
    }
  ],
  "title": "Tyr10 Modifications and Peptide Context Rewire GLP-1 Modulation of Amyloid-β42 Assembly",
  "title_text": "Tyr10 Modifications and Peptide Context Rewire GLP-1 Modulation of Amyloid-β42 Assembly",
  "type": "preprint",
  "updated_at": "2026-10-30T12:17:22Z",
  "url": "https://research.draconitic.com/paper/6r9eh7dy3ej3f",
  "venue": "ChemRxiv",
  "versions": []
}