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Alzheimer’s Disease Amyloid Peptides Interact with DNA, As Proved by Surface Plasmon Resonance
Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).ORCID iD: 0000-0002-1489-4098
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2012 (English)In: Current Alzheimer Research, ISSN 1567-2050, E-ISSN 1875-5828, Vol. 9, no 8, p. 924-934Article in journal (Refereed) Published
Abstract [en]

According to the amyloid hypothesis, abnormal processing of the β-amyloid precursor protein in Alzheimer's disease patients increases the production of β-amyloid toxic peptides, which, after forming highly aggregated fibrillar structures, lead to extracellular plaques formation, neuronal loss and dementia. However, a great deal of evidence has point to intracellular small oligomers of amyloid peptides, probably transient intermediates in the process of fibrillar structures formation, as the most toxic species. In order to study the amyloid-DNA interaction, we have selected here three different forms of the amyloid peptide: Aβ1-40, Aβ25-35 and a scrambled form of Aβ25-35. Surface Plasmon Resonance was used together with UV-visible spectroscopy, Electrophoresis and Electronic Microscopy to carry out this study. Our results prove that, similarly to the full length Aβ1-42, all conformations of toxic amyloid peptides, Aβ1-40 and Aβ25-35, may bind DNA. In contrast, the scrambled form of Aβ25-35, a non-aggregating and nontoxic form of this peptide, could not bind DNA. We conclude that although the amyloid-DNA interaction is closely related to the amyloid aggregation proneness, this cannot be the only factor which determines the interaction, since small oligomers of amyloid peptides may also bind DNA if their predominant negatively charged amino acid residues are previously neutralized.

Place, publisher, year, edition, pages
Bentham eBooks, 2012. Vol. 9, no 8, p. 924-934
Keywords [en]
Alzheimer, amyloid, DNA, surface plasmon resonance, Electron Microscopy, peptide, UV spectrum
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
URN: urn:nbn:se:mau:diva-14718DOI: 10.2174/156720512803251101ISI: 000309510400005PubMedID: 22631441Scopus ID: 2-s2.0-84867722125Local ID: 17737OAI: oai:DiVA.org:mau-14718DiVA, id: diva2:1418239
Available from: 2020-03-30 Created: 2020-03-30 Last updated: 2024-02-05Bibliographically approved

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Barrantes, Alejandro

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