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        <parTitl xml:lang="en">Data set for the Spectrochimica Acta Part A manuscript with the title "The structure of amyloid-beta(1-42) oligomers in membrane-mimetic environments"</parTitl>
        <IDNo agency="SND">doi-10-17045-sthlmuni-29910311-0</IDNo>
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    <citation>
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        <titl xml:lang="sv"></titl>
        <parTitl xml:lang="en">Data set for the Spectrochimica Acta Part A manuscript with the title "The structure of amyloid-beta(1-42) oligomers in membrane-mimetic environments"</parTitl>
        <IDNo agency="SND">doi-10-17045-sthlmuni-29910311-0</IDNo>
        <IDNo agency="DOI">https://doi.org/10.17045/STHLMUNI.29910311</IDNo>
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        <AuthEnty xml:lang="en" affiliation="Stockholm University">Kurysheva, Oleksandra</AuthEnty>
        <AuthEnty xml:lang="en" affiliation="Stockholm University">Barth, Andreas</AuthEnty>
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        <distDate xml:lang="en" date="2025-09-02" />
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      <abstract xml:lang="en" contentType="abstract">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.</abstract>
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