Protein structural changes induced by glutathione-coated CdS quantum dots as revealed by Trp phosphorescence (Articolo in rivista)

Type

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

Label

• Protein structural changes induced by glutathione-coated CdS quantum dots as revealed by Trp phosphorescence (Articolo in rivista) (literal)

Anno

• 2011-01-01T00:00:00+01:00 (literal)

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

• 10.1007/s00249-011-0736-x (literal)

Alternative label

• Gabellieri E, Cioni P, Balestreri E, Morelli E (2011)
  Protein structural changes induced by glutathione-coated CdS quantum dots as revealed by Trp phosphorescence
  in European biophysics journal
  (literal)

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

• Gabellieri E, Cioni P, Balestreri E, Morelli E (literal)

Pagina inizio

• 1237 (literal)

Pagina fine

• 1245 (literal)

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

• 40 (literal)

Rivista

• European biophysics journal (Rivista)

Note

• ISI Web of Science (WOS) (literal)

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

• Gabellieri E, IBF - CNR Cioni P, IBF - CNR Balestreri E, IBF - CNR Morelli E, IBF - CNR (literal)

Titolo

• Protein structural changes induced by glutathione-coated CdS quantum dots as revealed by Trp phosphorescence (literal)

Abstract

• We evaluated the potential of tryptophan (Trp) phosphorescence spectroscopy for investigating conformational states of proteins involved in interaction with nanoparticles. Characterization of protein-nanoparticle interaction is crucial in assessing biological hazards related to use of nanoparticles. We synthesized glutathione-coated CdS quantum dots (GSH-CdS), which exhibited an absorption peak at 366 nm, indicative of 2.4 nm core size. Chemical analysis of purified GSH-CdS suggested an average molecular formula of GSH18S56Cd60. Investigations were conducted on model proteins varying in terms of isoelectric point, degree of burial of the Trp probe, and quaternary structure. GSH-CdS fluorescence measurements showed improvement in nanoparticle quantum yield induced by protein interaction. Trp phosphorescence was used to examine the possible perturbations in the protein native fold induced by GSH-CdS. Phosphorescence lifetime measurements highlighted significant conformational changes in some proteins. Despite their small size, GSH-CdS appeared to interact with more than one protein molecule. Rough determination of the affinity of GSH-CdS for proteins was derived from the change in phosphorescence lifetime at increasing nanoparticle concentrations. The estimated affinities were comparable to those observed for specific protein-ligand interactions and suggest that protein-nanoparticle interaction may have a biological impact (literal)

Prodotto di

• Istituto di biofisica (IBF) (Istituto)
• Biofisica e biologia molecolare nello studio dei processi ambientali (TA.P04.030.001) (Modulo)
• Struttura e dinamica di proteine (MD.P01.008.001) (Modulo)

Autore CNR

• ELISABETTA MORELLI (Unità di personale interno)
• ETTORE BALESTRERI (Persona)
• PATRIZIA CIONI (Persona)
• EDI GABELLIERI (Unità di personale interno)

Incoming links:

Prodotto

• Istituto di biofisica (IBF) (Istituto)
• Struttura e dinamica di proteine (MD.P01.008.001) (Modulo)
• Biofisica e biologia molecolare nello studio dei processi ambientali (TA.P04.030.001) (Modulo)

Autore CNR di

• EDI GABELLIERI (Unità di personale interno)
• ETTORE BALESTRERI (Persona)
• ELISABETTA MORELLI (Unità di personale interno)
• PATRIZIA CIONI (Persona)

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

• European biophysics journal (Rivista)