2026-10-13 https://api.researchdata.se/oai-pmh

oai:researchdata.se:doi-10-17045-sthlmuni-29910311/0 2025-09-02 subject:ssif:30401 subject:ssif:304 subject:ssif:3 subject:ssif:106 subject:ssif:1 principal:slug:stockholm-university

info:eu-repo/semantics/other http://purl.org/dc/dcmitype/Dataset https://doi.org/10.17045/STHLMUNI.29910311 Data set for the Spectrochimica Acta Part A manuscript with the title "The structure of amyloid-beta(1-42) oligomers in membrane-mimetic environments" Oleksandra Kurysheva Nina Mann https://orcid.org/0000-0003-4986-0477 https://orcid.org/0000-0001-5784-7673 Medical Biotechnology (Focus on Cell Biology, (incl. Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy) Medicinsk bioteknologi (inriktn. mot cellbiologi (inkl. stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci) Biological Sciences Biologi Data published here is the basis for the manuscript for Spectrochimica Acta Part A with the title: The structure of amyloid-beta(1-42) oligomers in membrane-mimetic environments. Here, we demonstrate that Aβ42 oligomers preserve their β-sheet structure in aqueous solution and in a membrane-mimicking environment consisting of either anionic or zwitterionic membranes. Structure and Aβ42 aggregation kinetics were hardly affected by the presence of lipids, showing only slight effects observed during the initial oligomer formation at low temperatures. Our isotope-edited infrared experiments reveal that the backbone carbonyl of V18 residue is located in β-sheets in the presence and in the absence of lipids. Such insensitivity of Aβ42 to the presence of lipid vesicles suggests a distinct aggregation behaviour of Aβ42, compared to Aβ40. The data is in .DPT format, which can be viewed using any text editing program. https://creativecommons.org/licenses/by/4.0/ Stockholm University Stockholms universitet 2025-09-02T00:00:00Z