{
  "abstract": "Amyloid-β (Aβ) aggregation and associated structural changes are central features of Alzheimer’s disease (AD) pathology. In this study, we investigated the binding of α-halogenated curcumins, α-bromocurcumin and α-chlorocurcumin, to Aβ1-42 and examined their effects on the peptide secondary structure using fluorescence spectroscopy and circular dichroism (CD). Both α-halogenated curcumins interacted with Aβ1-42, but their binding properties differed from those of the parent curcumin. α-Chlorocurcumin exhibited a higher binding affinity for Aβ1-42 than curcumin, whereas α-bromocurcumin showed comparatively weaker binding. Temperature-dependent binding studies revealed that the association of α-halogenated curcumins with Aβ1-42 was influenced by temperature, with reduced binding affinity at higher temperatures. Thermodynamic analysis demonstrated favorable free-energy changes for the interactions and revealed that α-halogenation altered the relative enthalpic and entropic contributions to Aβ1-42 binding. CD analysis further showed that binding of the curcumin altered the secondary structure of Aβ1-42. These structural changes were more pronounced in the presence of the α-halogenated derivatives, indicating that halogen substitution influences the interaction and conformational response of Aβ1-42. Molecular docking analysis provided additional insight into the possible binding modes and predicted intermolecular contacts between the α-halogenated curcumin and Aβ1-42. Overall, the findings demonstrate that α-halogenation modulates the binding and structural effects of curcumin derivatives on Aβ1-42, with α-chlorocurcumin exhibiting particularly favorable binding characteristics. These findings provide a basis for further investigation of α-halogenated curcumins as potential modulators of Aβ-related molecular processes associated with AD.",
  "abstract_shown": true,
  "affiliations": [
    "Department of Life Sciences, College of Science, Alfaisal University, Riyadh 11533, Saudi Arabia",
    "College of Medicine, Alfaisal University, Riyadh 11533, Saudi Arabia",
    "Department of Biochemistry, School of Life Sciences, University of Hyderabad, Hyderabad 500 046, India",
    "Tissue/Organ Bioengineering & BioMEMS Laboratory, Organ Transplant Centre of Excellence (TR & I-Dept), King Faisal Specialist Hospital & Research Centre, Riyadh 11211, Saudi Arabia",
    "Department of Chemistry, Penn State Scranton, Dunmore, PA 18512, USA",
    "Department of Chemistry, College of Science, Alfaisal University, Riyadh 11533, Saudi Arabia"
  ],
  "article_type": "research article",
  "arxiv": null,
  "author_total": 8,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "Mateen A. Khan",
      "orcid": "0000-0002-2300-4595"
    },
    {
      "affs": [
        1
      ],
      "name": "Raja Chinnappan",
      "orcid": "0000-0002-2288-4287"
    },
    {
      "affs": [
        2
      ],
      "name": "Sowmya Andole",
      "orcid": "0000-0002-8518-1802"
    },
    {
      "affs": [
        2
      ],
      "name": "Mohd. Akif",
      "orcid": "0000-0001-8462-7166"
    },
    {
      "affs": [
        3
      ],
      "name": "Tanveer Ahmad Mir"
    },
    {
      "affs": [
        1
      ],
      "name": "Ahmed Yaqinuddin",
      "orcid": "0000-0001-7536-910X"
    },
    {
      "affs": [
        4
      ],
      "name": "Phuong-T T. Pham"
    },
    {
      "affs": [
        5
      ],
      "name": "Mamoun M. Bader",
      "orcid": "0000-0002-4743-6747"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/4ex8pvds339qx.bib",
  "cited_by": 0,
  "doi": "10.3390/ijms27209355",
  "fulltext_url": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13705457/?tool=EBI",
  "id": "4ex8pvds339qx",
  "issns": [
    "1422-0067"
  ],
  "landing_url": "https://www.mdpi.com/1422-0067/27/20/9355",
  "language": "eng",
  "licence": "CC-BY-4.0",
  "licence_label": "CC BY 4.0",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "openalex",
      "2737|Alzheimer's disease research and treatments"
    ]
  ],
  "openalex": "W7223259657",
  "pdf_url": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13705457/pdf/?tool=EBI",
  "pmcid": "PMC13705457",
  "pmid": null,
  "published": "2026-10-01",
  "publisher": "MDPI AG",
  "ris": "https://research.draconitic.com/paper/4ex8pvds339qx.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:18:57Z",
      "native_id": "10.3390/ijms27209355",
      "source": "crossref",
      "url": "https://www.mdpi.com/1422-0067/27/20/9355"
    },
    {
      "first_seen": "2026-10-30T12:21:47Z",
      "native_id": "PMC:PMC13705457",
      "source": "europepmc",
      "url": "https://europepmc.org/article/PMC/PMC13705457"
    }
  ],
  "subjects": [
    {
      "field": "medicine",
      "origin": "openalex:2737|Alzheimer's disease research and treatments",
      "subfield": "physiology"
    }
  ],
  "title": "α-Halogenated Curcumins Enhance the Binding Affinity and Induced Structural Alterations to Amyloid-β Protein in Alzheimer’s Disease",
  "title_text": "α-Halogenated Curcumins Enhance the Binding Affinity and Induced Structural Alterations to Amyloid-β Protein in Alzheimer’s Disease",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:21:47Z",
  "url": "https://research.draconitic.com/paper/4ex8pvds339qx",
  "venue": "International Journal of Molecular Sciences",
  "versions": []
}