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Naji, M. |
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Motta, Antonella |
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Aletan, Dirar |
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Mohamed, Tarek |
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Ertürk, Emre |
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Taccardi, Nicola |
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Kononenko, Denys |
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Petrov, R. H. | Madrid |
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Alshaaer, Mazen | Brussels |
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Bih, L. |
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Casati, R. |
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Muller, Hermance |
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Kočí, Jan | Prague |
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Šuljagić, Marija |
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Kalteremidou, Kalliopi-Artemi | Brussels |
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Azam, Siraj |
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Ospanova, Alyiya |
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Blanpain, Bart |
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Ali, M. A. |
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Popa, V. |
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Rančić, M. |
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Ollier, Nadège |
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Azevedo, Nuno Monteiro |
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Landes, Michael |
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Rignanese, Gian-Marco |
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Ke, Pu Chun
in Cooperation with on an Cooperation-Score of 37%
Topics
Publications (7/7 displayed)
- 2017Cofibrillization of pathogenic and functional amyloid proteins with gold nanoparticles against amyloidogenesiscitations
- 2016Inhibition of hIAPP amyloid aggregation and pancreatic β-cell toxicity by OH-terminated PAMAM dendrimercitations
- 2015PAMAM dendrimers and graphene: materials for removing aromatic contaminants from watercitations
- 2013Exploiting the physicochemical properties of dendritic polymers for environmental and biological applicationscitations
- 2012Understanding dendritic polymer-hydrocarbon interactions for oil dispersioncitations
- 2008Single-Molecule Dendrimer-Hydrocarbon Interactioncitations
- 2007Single-molecule study of dendrimer-hydrocarbon interaction
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article
Cofibrillization of pathogenic and functional amyloid proteins with gold nanoparticles against amyloidogenesis
Abstract
Biomimetic nanocomposites and scaffolds hold the key to a wide range of biomedical applications. Here we show, for the first time, a facile scheme of cofibrillizing pathogenic and functional amyloid fibrils via gold nanoparticles (AuNPs) and their applications against amyloidogenesis. This scheme was realized by β-sheet stacking between human islet amyloid polypeptide (IAPP) and the β-lactoglobulin “corona” of the AuNPs, as revealed by transmission electron microscopy, 3D atomic force microscopy, circular dichroism spectroscopy, and molecular dynamics simulations. The biomimetic AuNPs eliminated IAPP toxicity, enabled X-ray destruction of IAPP amyloids, and allowed dark-field imaging of pathogenic amyloids and their immunogenic response by human T cells. In addition to providing a viable new nanotechnology against amyloidogenesis, this study has implications for understanding the in vivo cross-talk between amyloid proteins of different pathologies.