Journal
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
Volume 15, Issue 44, Pages 19129-19133Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c3cp52732h
Keywords
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Funding
- Dept. of Biotechnology, Govt. of India [BT/53/NE/TBP/2010]
- Israel Science Foundation [ISF1461/10]
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Small amyloid-beta (A beta) 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), A beta 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.
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