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PEGylated phospholipid nanomicelles interact with beta-amyloid((1-42)) and mitigate its beta-sheet formation, aggregation and neurotoxicity in vitro
Link to Journal Abstract
beta-Amyloid (Abeta) is a hydrophobic peptide that drives the pathogenesis of Alzheimer's disease (AD) due to its aberrant aggregation. Inhibition of Abeta aggregation process is one of the most promising strategies for therapeutic intervention in AD. Here, we demonstrate that sterically stabilized (PEGylated) phospholipid nanomicelles (SSM) are effective in mitigating Abeta-42 aggregation using several deterministic techniques such as (1) Turbidimetry (2) Congo red binding (3) Thioflavine-T binding (4) Laser light scattering and (5) Electron Microscopy. alpha-Helicity of Abeta-42 is significantly augmented in the presence of SSM as demonstrated by circular dichroism (p<0.05). Cytotoxicity studies, employing human neuroblastoma SHSY-5Y cells, established that PEGylated phospholipid associated peptide demonstrated significantly lower neurotoxicity compared to lipid untreated Abeta-42 (p<0.05). Collectively, our results establish that PEGylated phospholipids abrogate transformation of Abeta-42 to amyloidogenic beta-sheeted form and impart neuroprotection in vitro. This study provides a foundation for designing nanoconstructs of PEGylated phospholipid nanomicelles in conjunction with a therapeutic agent for multitargeting the different pathophysiologies associated with AD.
This ex vivo study showed that biocompatible phospholipid nanomicelles about 14 nm in diameter inhibit the aggregation of a protein associated with Alzheimer's disease.
Peer Reviewed Journal Article
Peptides. 2006 Nov;27(11):2858-66. Epub 2006 Jun 9
Pai AS, Rubinstein I, Onyuksel H
Last updated on September 25, 2007
This work is supported in part by the Nanoscale Science and Engineering Initiative of the National Science Foundation
under NSF Award Number EEC-0118007.
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