PUMA
Istituto di Biofisica     
Gabellieri E., Cioni P., Balestrieri E., Morelli E. Protein structural changes induced by glutathione-coated CdS quantum dots as revealed by Trp phosphorescence. In: European Biophysics Journal With Biophysics Letters, vol. 249 pp. 736 - 745. elsevier, 2011.
 
 
Abstract
(English)
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 puriWed 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 Xuorescence 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 signiWcant conformational changes in some proteins. Despite their small size, GSH-CdS appeared to interact with more than one protein molecule. Rough determination of the aYnity of GSH-CdS for proteins was derived from the change in phosphorescence lifetime at increasing nanoparticle concentrations. The estimated aYnities were comparable to those observed for speciWc protein- ligand interactions and suggest that protein-nanoparticle interaction may have a biological impact.
DOI: DOI 10.1007/s00249-011-0736-x
Subject Glutathione-coated CdS quantum dots Protein-nanoparticle interaction Room-temperature phosphorescence Fluorescence of nanopartic


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