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The influence of a GATG (gallic acid-triethylene glycol) dendrimer decorated with 27 terminal morpholine groups ([G3]-Mor) on the aggregation process of Alzheimer's peptide has been investigated. Amyloid fibrils were formed from the Aβ 1-28 peptide and the process was monitored by a ThT assay, changes in CD spectra, and transmission electron microscopy. In the presence of [G3]-Mor, more fibrils were built and the process significantly accelerated compared with a control. The cytotoxicity of (1) Aβ and (2) the system [G3]-Mor/Aβ was monitored at different stages of the aggregation process. Prefibrillar species were more toxic than mature fibrils. [G3]-Mor significantly reduced the toxicity of Aβ, probably because of lowering the amount of prefibrillar forms in the system by speeding up the process of fibril formation. In this study, GATG dendrimer decorated with 27 terminal morpholine groups was able to reduce beta-amyloid fibril formation, which might represent a new method to address the key pathology in Alzheimer's disease. Copyright © 2012 Elsevier Inc. All rights reserved.


Barbara Klajnert, Tomasz Wasiak, Maksim Ionov, Marcos Fernandez-Villamarin, Ana Sousa-Herves, Juan Correa, Ricardo Riguera, Eduardo Fernandez-Megia. Dendrimers reduce toxicity of Aβ 1-28 peptide during aggregation and accelerate fibril formation. Nanomedicine : nanotechnology, biology, and medicine. 2012 Nov;8(8):1372-8

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PMID: 22465497

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