Klajnert, BarbaraWasiak, TomaszIonov, MaksimFernández Villamarín, MarcosSousa Hervés, AnaCorrea, JuanRiguera Vega, RicardoFernández Megía, Eduardo2018-07-062018-07-062012-11Klajnert, B., Wasiak, T., Ionov, M., Fernandez-Villamarin, M., Sousa-Herves, A., & Correa, J. et al. (2012). Dendrimers reduce toxicity of Aβ 1-28 peptide during aggregation and accelerate fibril formation. Nanomedicine: Nanotechnology, Biology And Medicine, 8(8), 1372-1378. doi: 10.1016/j.nano.2012.03.0051549-9634http://hdl.handle.net/10347/16971The 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 formationeng© 2012 Elsevier B.V. This manuscript version is made available under the CC-BY-NC-ND 4.0 license (http:// creativecommons.org/licenses/by-nc-nd/4.0/)DendrimerAlzheimer's diseaseAβ 1-28Amyloid peptidejournal article10.1016/j.nano.2012.03.005open access