{
  "abstract": "The aggregation of amyloid-{beta} (A{beta}) peptides into insoluble deposits is a characteristic hallmark of Alzheimer's disease (AD) and related neurodegenerative disorders. While AD is the most common cause of dementia, there are currently no disease-modifying treatments which are both affordable and adverse-free. In this study, we report that melanin, a pigment which is commonly found in nature and is abundant in parts of the human brain, suppresses the aggregation of the 42-amino acid A{beta} variant (A{beta}42). Using biophysical and biochemical techniques, we show that melanin delays A{beta}42 aggregation while also reducing the amount of A{beta}42 that converts into aggregates. Using thioflavin T assays paired with chemical kinetics, we characterised the melanin-induced inhibition of A{beta}42 aggregation in vitro. Using MALDI-MS, we elucidate the molecular basis of this effect by showing that melanin prevents A{beta}42 dimerisation. We then demonstrate that melanin also reverts the aggregation process by dissolving pre-formed A{beta}42 fibrils. Finally, we show that melanin reduces A{beta}42 aggregation and rescues A{beta}42 toxicity in an SH-SY5Y neuroblastoma cell model. Our study shows that melanin disrupts the aggregation and cytotoxicity of A{beta}42, and suggests that compounds derived from human metabolites may offer promising avenues to combat amyloid formation.",
  "abstract_shown": true,
  "affiliations": [
    "Yusuf Hamied Department of Chemistry, University of Cambridge"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 4,
  "authors": [
    {
      "name": "A. Röntgen"
    },
    {
      "name": "J. L. Heise"
    },
    {
      "name": "M. Vendruscolo"
    },
    {
      "affs": [
        0
      ],
      "name": "Z. Toprakcioglu"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/85c2hb96jrp6r.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.09.01.748646",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.09.01.748646v1.full",
  "id": "85c2hb96jrp6r",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.09.01.748646v1",
  "language": null,
  "licence": "CC-BY-NC",
  "licence_label": "CC BY-NC",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by-nc/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "biorxiv",
      "biophysics"
    ],
    [
      "openalex",
      "2737|Alzheimer's disease research and treatments"
    ]
  ],
  "openalex": "W7207815796",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.09.01.748646v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-01",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/85c2hb96jrp6r.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:18:37Z",
      "native_id": "10.64898/2026.09.01.748646",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.09.01.748646v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "biorxiv:biophysics",
      "subfield": "biophysics"
    }
  ],
  "title": "Melanin Suppresses Aβ Aggregation and Toxicity",
  "title_text": "Melanin Suppresses Aβ Aggregation and Toxicity",
  "type": "preprint",
  "updated_at": "2026-10-30T12:18:37Z",
  "url": "https://research.draconitic.com/paper/85c2hb96jrp6r",
  "venue": "bioRxiv",
  "versions": []
}