Dynamics of a Globular Protein Adsorbed to Liposomal Nanoparticles (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Dynamics of a Globular Protein Adsorbed to Liposomal Nanoparticles (Articolo in rivista) (literal)

Anno

• 2014-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1021/ja507310m (literal)

Alternative label

• Ceccon, Alberto; Lelli, Moreno; D'Onofrio, Mariapina; Molinari, Henriette; Assfalg, Michael (2014)
  Dynamics of a Globular Protein Adsorbed to Liposomal Nanoparticles
  in Journal of the American Chemical Society (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Ceccon, Alberto; Lelli, Moreno; D'Onofrio, Mariapina; Molinari, Henriette; Assfalg, Michael (literal)

Pagina inizio

• 13158 (literal)

Pagina fine

• 13161 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 136 (literal)

Rivista

• Journal of the American Chemical Society (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali

• 4 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 38 (literal)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• University of Verona; Centre National de la Recherche Scientifique (CNRS); Consiglio Nazionale delle Ricerche (CNR) (literal)

Titolo

• Dynamics of a Globular Protein Adsorbed to Liposomal Nanoparticles (literal)

Abstract

• A solution-state NMR method is proposed to investigate the dynamics of proteins that undergo reversible association with nanoparticles (NPs). We applied the recently developed dark-state exchange saturation transfer experiment to obtain residue-level dynamic information on a NP-adsorbed protein in the form of transverse spin relaxation rates, R-2(bound). Based on dynamic light scattering, fluorescence, circular dichroism, and NMR spectroscopy data, we show that the test protein, human liver fatty acid binding protein, interacts reversibly and peripherally with liposomal NPs without experiencing significant structural changes. The significant but modest saturation transfer from the bound state observed at 14.1 and 23.5 T static magnetic fields, and the small determined R-2(bound) values were consistent with a largely unrestricted global motion at the lipid surface. Amino acid residues displaying faster spin relaxation mapped to a region that could represent the epitope of interaction with an extended phospholipid chain constituting the protein anchor. These results prove that atomic-resolution protein dynamics is accessible even after association with NPs, supporting the use of saturation transfer methods as powerful tools in bionanoscience. (literal)

Prodotto di

• Strutturistica NMR di proteine legate a processi patologici (PM.P01.026.003) (Modulo)
• Istituto per lo studio delle macromolecole (ISMAC) (Istituto)

Autore CNR

• HENRIETTE MOLINARI (Unità di personale esterno)
• LAURA GIUDITTA RAGONA (Unità di personale interno)

Incoming links:

Prodotto

• Istituto per lo studio delle macromolecole (ISMAC) (Istituto)
• Strutturistica NMR di proteine legate a processi patologici (PM.P01.026.003) (Modulo)

Autore CNR di

• LAURA GIUDITTA RAGONA (Unità di personale interno)
• HENRIETTE MOLINARI (Unità di personale esterno)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Journal of the American Chemical Society (Rivista)