Citrate-stabilized Gold Nanoparticles hinder fibrillogenesis of a pathologic variant of β2-microglobulin
| Autor: | Loredana Marchese, Sara Raimondi, Vittorio Bellotti, Federico Fogolari, Stefano Corni, Sofia Giorgetti, Giovanni Palmisano, Alessandra Corazza, Maurizio Ballico, Stefano Zanini, Paolo Bertoncin, Palma Mangione, Cristina Cantarutti, Giorgia Brancolini, Gennaro Esposito |
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| Přispěvatelé: | Cantarutti, Cristina, Raimondi, Sara, Brancolini, Giorgia, Corazza, Alessandra, Giorgetti, Sofia, Ballico, Maurizio, Zanini, Stefano, Palmisano, Giovanni, Bertoncin, Paolo, Marchese, Loredana, Patrizia Mangione, P., Bellotti, Vittorio, Corni, Stefano, Fogolari, Federico, Esposito, Gennaro |
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
Beta-2 microglobulin
Chemistry Nanotechnology Fibrillogenesis 02 engineering and technology 010402 general chemistry 021001 nanoscience & nanotechnology Fibril 01 natural sciences 0104 chemical sciences chemistry.chemical_compound Protein structure Colloidal gold Nanoparticles. Amyloidogenic proteins. Protein NMR. Protein-Nanoparticle interactions Agarose gel electrophoresis Biophysics General Materials Science Thioflavin Materials Science (all) Asparagine 0210 nano-technology |
| Zdroj: | Nanoscale 9 (2017): 3941–3951. doi:10.1039/c6nr09362k info:cnr-pdr/source/autori:Cantarutti C.; Raimondi S.; Brancolini G.; Corazza A.; Giorgetti S.; Ballico M.; Zanini S.; Palmisano G.; Bertoncin P.; Marchese L.; Patrizia Mangione P.; Bellotti V.; Corni S.; Fogolari F.; Esposito G./titolo:Citrate-stabilized gold nanoparticles hinder fibrillogenesis of a pathological variant of ?2-microglobulin/doi:10.1039%2Fc6nr09362k/rivista:Nanoscale (Print)/anno:2017/pagina_da:3941/pagina_a:3951/intervallo_pagine:3941–3951/volume:9 |
| Popis: | Nanoparticles have repeatedly been shown to enhance fibril formation when assayed with amyloidogenic proteins. Recently, however, evidence casting some doubt about the generality of this conclusion started to emerge. Therefore, to investigate further the influence of nanoparticles on the fibrillation process, we used a naturally occurring variant of the paradigmatic amyloidogenic protein β2-microglobulin (β2m), namely D76N β2m where asparagine replaces aspartate at position 76. This variant is responsible for aggressive systemic amyloidosis. After characterizing the interaction of the variant with citrate-stabilized gold nanoparticles (Cit-AuNPs) by NMR and modeling, we analyzed the fibril formation by three different methods: thioflavin T fluorescence, native agarose gel electrophoresis and transmission electron microscopy. The NMR evidence indicated a fast-exchange interaction involving preferentially specific regions of the protein that proved, by subsequent modeling, to be consistent with a dimeric adduct interacting with Cit-AuNPs. The fibril detection assays showed that AuNPs are able to hamper D76N β2m fibrillogenesis through an effective interaction that competes with protofibril formation or recruitment. These findings open promising perspectives for the optimization of the nanoparticle surface to design tunable interactions with proteins. |
| Databáze: | OpenAIRE |
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