Giovanni Maglia

Margarida Gairí

Mariam Bayoumi

Martí Ninot-Pedrosa

Montserrat Serra-Batiste

Natàlia Carulla

Significance
          Numerous reports indicate that amyloid-β peptide (Aβ) oligomers, considered the pathogenic molecular form of Aβ in Alzheimer´s disease (AD), exert their neurotoxicity within the membrane. Therefore, it is critical to characterize them in such an environment. Here, we worked with two major Aβ variants and handled them as if they were membrane proteins. By doing so, we found that the Aβ variant most strongly linked to AD assembled into stable Aβ oligomers that adopted a specific structure and incorporated into membranes as pores, a feature linked to neurotoxicity. Having access to pore-forming Aβ oligomers with such a specific structure offers unique opportunities to fully characterize them and establish their involvement in AD.</jats:p

Aβ42 assembles into specific β-barrel pore-forming oligomers in membrane-mimicking environments

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