Amyloid transition of ubiquitin on silver nanoparticles produced by pulsed laser ablation in liquid as a function of stabilizer and single-point mutations (Articolo in rivista)

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Label
  • Amyloid transition of ubiquitin on silver nanoparticles produced by pulsed laser ablation in liquid as a function of stabilizer and single-point mutations (Articolo in rivista) (literal)
Anno
  • 2014-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/chem.201402934 (literal)
Alternative label
  • Mangini V.; Dell'Aglio M.; Stradis A.D.; Giacomo A.D.; Pascale O.D.; Natile G.; Arnesano F. (2014)
    Amyloid transition of ubiquitin on silver nanoparticles produced by pulsed laser ablation in liquid as a function of stabilizer and single-point mutations
    in Chemistry - A European Journal
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Mangini V.; Dell'Aglio M.; Stradis A.D.; Giacomo A.D.; Pascale O.D.; Natile G.; Arnesano F. (literal)
Pagina inizio
  • 10745 (literal)
Pagina fine
  • 10751 (literal)
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  • http://www.scopus.com/inward/record.url?eid=2-s2.0-84906046422&partnerID=q2rCbXpz (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 20 (literal)
Rivista
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  • 34 (literal)
Note
  • Scopu (literal)
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  • Department of Chemistry, University of Bari Aldo Moro, via Orabona, 4, 70125, Bari, Italy; CNR-IMIP, Section of Bari, via Amendola 122/D, 70126, Bari, Italy; CNR-IVV, Section of Bari, via Amendola 165A, 70126, Bari, Italy (literal)
Titolo
  • Amyloid transition of ubiquitin on silver nanoparticles produced by pulsed laser ablation in liquid as a function of stabilizer and single-point mutations (literal)
Abstract
  • The interaction of nanoparticles with proteins has emerged as a key issue in addressing the problem of nanotoxicity. We investigated the interaction of silver nanoparticles (AgNPs), produced by laser ablation with human ubiquitin (Ub), a protein essential for degradative processes in cells. The surface plasmon resonance peak of AgNPs indicates that Ub is rapidly adsorbed on the AgNP surface yielding a protein corona; the Ub-coated AgNPs then evolve into clusters held together by an amyloid form of the protein, as revealed by binding of thioflavin T fluorescent dye. Transthyretin, an inhibitor of amyloid-type aggregation, impedes aggregate formation and disrupts preformed AgNP clusters. In the presence of sodium citrate, a common stabilizer that confers an overall negative charge to the NPs, Ub is still adsorbed on the AgNP surface, but no clustering is observed. Ub mutants bearing a single mutation at one edge ? strand (i.e. Glu16Val) or in loop (Glu18Val) behave in a radically different manner. Human ubiquitin forms amyloids on the surface of silver nanoparticles produced by laser ablation, which induce clustering of the nanoparticles and thioflavin T fluorescence. In the presence of sodium citrate as a stabilizer, ubiquitin only forms a protein corona. A single mutation (Glu16Val) at one edge ? strand of the protein can deeply influence the amyloid transition (see figure). © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. (literal)
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