Abstract
Small amyloid-β (Aβ) oligomers have much higher membrane affinity compared to the monomers, but the structural origin of this functional change is not understood. We show that as monomers assemble into small n-mers (n < 10), Aβ acquires a tertiary fold that is consistent with the mature fibrils. This is an early and defining transition for the aggregating peptide, and possibly underpins its altered bioactivity.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amyloid beta-Peptides / chemical synthesis
-
Amyloid beta-Peptides / chemistry
-
Amyloid beta-Peptides / metabolism*
-
Fluorescein / chemistry
-
Fluorescence Resonance Energy Transfer
-
Peptide Fragments / chemical synthesis
-
Peptide Fragments / chemistry
-
Peptide Fragments / metabolism
-
Phosphatidylcholines / chemistry
-
Protein Folding
-
Protein Structure, Secondary
Substances
-
1-myristoyl-2-(12-((5-dimethylamino-1-naphthalenesulfonyl)amino)dodecanoyl)-sn-glycero-3-phosphocholine
-
Amyloid beta-Peptides
-
Peptide Fragments
-
Phosphatidylcholines
-
amyloid beta-protein (1-40)
-
Fluorescein