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Cline, Erika N. ; Das, Arighno ; Bicca, Maíra Assunção ; Mohammad, Saad N. ; Schachner, Luis F. ; Kamel, Josette M. ; DiNunno, Nadia ; Weng, Anthea ; Paschall, Jacob D. ; Bu, Riana Lo ; et al ( , Journal of Neurochemistry)
Abstract Amyloid β oligomers (AβOs) accumulate early in Alzheimer's disease (
AD ) and experimentally cause memory dysfunction and the major pathologies associated withAD , for example, tau abnormalities, synapse loss, oxidative damage, and cognitive dysfunction. In order to develop the most effective AβO‐targeting diagnostics and therapeutics, the AβO structures contributing toAD ‐associated toxicity must be elucidated. Here, we investigate the structural properties and pathogenic relevance of AβOs stabilized by the bifunctional crosslinker 1,5‐difluoro‐2,4‐dinitrobenzene (DFDNB ). We find thatDFDNB stabilizes synthetic Aβ in a soluble oligomeric conformation. WithDFDNB , solutions of Aβ that would otherwise convert to large aggregates instead yield solutions of stable AβOs, predominantly in the 50–300kD a range, that are maintained for at least 12 days at 37°C. Structures were determined by biochemical and native top–down mass spectrometry analyses. Assayed in neuronal cultures and i.c.v.‐injected mice, theDFDNB ‐stabilized AβOs were found to induce tau hyperphosphorylation, inhibit choline acetyltransferase, and provoke neuroinflammation. Most interestingly,DFDNB crosslinking was found to stabilize an AβO conformation particularly potent in inducing memory dysfunction in mice. Taken together, these data support the utility ofDFDNB crosslinking as a tool for stabilizing pathogenic AβOs in structure‐function studies.image