Thermally induced denaturation and aggregation of BLG-A: effect of the Cu2+ and Zn2+ metal ions (Articolo in rivista)

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  • Thermally induced denaturation and aggregation of BLG-A: effect of the Cu2+ and Zn2+ metal ions (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Alternative label
  • Stirpe, A; Rizzuti, B; Pantusa, M; Bartucci, R; Sportelli, L; Guzzi, R (2008)
    Thermally induced denaturation and aggregation of BLG-A: effect of the Cu2+ and Zn2+ metal ions
    in European biophysics journal
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Stirpe, A; Rizzuti, B; Pantusa, M; Bartucci, R; Sportelli, L; Guzzi, R (literal)
Pagina inizio
  • 1351 (literal)
Pagina fine
  • 1360 (literal)
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  • 37 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
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  • \"[Stirpe, A.; Pantusa, M.; Bartucci, R.; Sportelli, L.; Guzzi, R.] Univ Calabria, Dipartimento Fis, Lab Biofis Mol, I-87036 Arcavacata Di Rende, CS, Italy; [Stirpe, A.; Pantusa, M.; Bartucci, R.; Sportelli, L.; Guzzi, R.] Univ Calabria, Unita CNISM, I-87036 Arcavacata Di Rende, CS, Italy; [Rizzuti, B.] Univ Calabria, Dipartimento Fis, Lab Licryl CNR INFM, I-87036 Arcavacata Di Rende, CS, Italy (literal)
Titolo
  • Thermally induced denaturation and aggregation of BLG-A: effect of the Cu2+ and Zn2+ metal ions (literal)
Abstract
  • There is growing evidence that metal ions can accelerate the aggregation process of several proteins. This process, associated with several neuro-degenerative diseases, has been reported also for non-pathological proteins. In the present work, the effects of copper and zinc ions on the denaturation and aggregation processes of beta-lactoglobulin A (BLG-A) are investigated by differential scanning calorimetry (DSC), fluorescence, electron paramagnetic resonance (EPR) and optical density. The DSC profiles reveal that the thermal behaviour of BLG-A is a complex process, strongly dependent on the protein concentration. For concentrations <= 0.13 mM, the thermogram shows an endothermic peak at 84.3 degrees C, corresponding to denaturation; for concentrations > 0.13 mM an exothermic peak also appears, above 90 degrees C, related to the aggregation of the denaturated BLG-A molecules. The thioflavin T fluorescence indicates that the thermally induced aggregates show fibrillar features. The presence of either equimolar Cu2+ or Zn2+ ions in the protein solution has different effects. In particular, copper binds to the protein in the native state, as evidenced by EPR experiments, and destabilizes BLG-A by decreasing the denaturation temperature by about 10 degrees C, whereas zinc ions probably perturb the partially denaturated state of the protein. The kinetics of BLG-A aggregation shows that both metal ions abolish the lag phase before the aggregation starts. Moreover, the rate of the process is 4.6-fold higher in the presence of copper, whereas the effect of zinc is negligible. The increase of the aggregation rate, induced by copper, may be due to a site-specific binding of the metal ion on the protein. (literal)
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