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Aβ(1-42) tetramer and octamer structures reveal edge conductivity pores as a mechanism for membrane damage.

Abstract：

:Formation of amyloid-beta (Aβ) oligomer pores in the membrane of neurons has been proposed to explain neurotoxicity in Alzheimer's disease (AD). Here, we present the three-dimensional structure of an Aβ oligomer formed in a membrane mimicking environment, namely an Aβ(1-42) tetramer, which comprises a six stranded β-sheet core. The two faces of the β-sheet core are hydrophobic and surrounded by the membrane-mimicking environment while the edges are hydrophilic and solvent-exposed. By increasing the concentration of Aβ(1-42) in the sample, Aβ(1-42) octamers are also formed, made by two Aβ(1-42) tetramers facing each other forming a β-sandwich structure. Notably, Aβ(1-42) tetramers and octamers inserted into lipid bilayers as well-defined pores. To establish oligomer structure-membrane activity relationships, molecular dynamics simulations were carried out. These studies revealed a mechanism of membrane disruption in which water permeation occurred through lipid-stabilized pores mediated by the hydrophilic residues located on the core β-sheets edges of the oligomers.

journal_name

Nat Commun

journal_title

Nature communications

authors

Ciudad S,Puig E,Botzanowski T,Meigooni M,Arango AS,Do J,Mayzel M,Bayoumi M,Chaignepain S,Maglia G,Cianferani S,Orekhov V,Tajkhorshid E,Bardiaux B,Carulla N

doi

10.1038/s41467-020-16566-1

subject

Has Abstract

pub_date

2020-06-15 00:00:00

pages

3014

issue

1

issn

2041-1723

pii

10.1038/s41467-020-16566-1

journal_volume

11

pub_type

杂志文章

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