http://www.cnr.it/ontology/cnr/individuo/prodotto/ID9961
Protein structural changes induced by glutathione-coated CdS quantum dots as revealed by Trp phosphorescence (Articolo in rivista)
- Type
- 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)
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- 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)
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