<p dir="ltr">Data published here is the basis for the manuscript for Spectrochimica Acta Part A with the title:</p><p><br></p><p dir="ltr"><i>The structure of amyloid-beta(1-42) oligomers in membrane-mimetic environments.</i></p><p><br></p><p dir="ltr">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.</p><p><br></p><p dir="ltr">The data is in .DPT format, which can be viewed using any text editing program.</p>
Oleksandra Kurysheva, Nina Mann, Uliana Afonina, Andreas Barth, The structure of amyloid-β (1–42) oligomers in membrane-mimetic environments, Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 2025, 126875, ISSN 1386-1425, https://doi.org/10.1016/j.saa.2025.126875
Affiliation (institution of first SU-affiliated author)
431 Institutionen för biokemi och biofysik (DBB) | Department of Biochemistry and Biophysics (DBB)