Fig. 5: Structural analysis of three polymorphs of Aβ42-4b fibrils. | Nature Communications

Fig. 5: Structural analysis of three polymorphs of Aβ42-4b fibrils.

From: An O-glycopeptide participates in the formation of distinct Aβ42 fibril structures and attenuates Aβ42 neurotoxicity

Fig. 5

a Structures of the four subtypes (top) and the primary sequence with beta-strands formed in the fibril structures (bottom). b Structure overlay of subtype 1 and subtype 3. c One layer of Aβ42-4b-P1 with subtype chains colored. The zoomed-in views of the side-chain interactions between different chains in Aβ42-4b-P1 are shown at the bottom. d Structural comparison of two paired subtype 1 chains and Aβ42 wild-type fibrils (PDB: 2NAO). e Structure overlay of Aβ42-4b-P1, P2, and P3 with zoomed-in views of residues V12-K16.

Back to article page