X-ray absorption spectroscopy data show different metal binding site structures in beta-amyloid peptides according to whether they are complexed with Cu(2+)or Zn2+ ions. While the geometry around copper is stably consistent with an intra-peptide binding with three metal-coordinated Histidine residues, the zinc coordination mode depends on specific solution conditions. In particular, different sample preparations are seen to lead to different geometries around the absorber that are compatible with either an intra- or an inter-peptide coordination mode. This result reinforces the hypothesis that assigns different physiological roles to the two metals, with zinc favoring peptide aggregation and, as a consequence, plaque formation.

Stellato, F., Menestrina, G., Dalla Serra, M., Potrich, C., Tomazzolli, R., Meyer Klaucke, W., et al. (2006). Metal binding in amyloid beta-peptides shows intra- and inter-peptide coordination modes. EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, 35(4), 340-351 [10.1007/s00249-005-0041-7].

Metal binding in amyloid beta-peptides shows intra- and inter-peptide coordination modes

Stellato, F;MORANTE, SILVIA
2006

Abstract

X-ray absorption spectroscopy data show different metal binding site structures in beta-amyloid peptides according to whether they are complexed with Cu(2+)or Zn2+ ions. While the geometry around copper is stably consistent with an intra-peptide binding with three metal-coordinated Histidine residues, the zinc coordination mode depends on specific solution conditions. In particular, different sample preparations are seen to lead to different geometries around the absorber that are compatible with either an intra- or an inter-peptide coordination mode. This result reinforces the hypothesis that assigns different physiological roles to the two metals, with zinc favoring peptide aggregation and, as a consequence, plaque formation.
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore FIS/07 - Fisica Applicata(Beni Culturali, Ambientali, Biol.e Medicin)
English
amyloid beta protein; copper ion; histidine; metal complex; zinc ion; article; binding site; geometry; interpeptide coordination mode; intrapeptide coordination mode; metal binding; protein aggregation; roentgen spectroscopy; senile plaque; Amyloid beta-Protein; Cations, Divalent; Copper; Fourier Analysis; Histidine; Imidazoles; Models, Molecular; Protein Binding; Protein Conformation; Spectrum Analysis; X-Rays; Zinc
Stellato, F., Menestrina, G., Dalla Serra, M., Potrich, C., Tomazzolli, R., Meyer Klaucke, W., et al. (2006). Metal binding in amyloid beta-peptides shows intra- and inter-peptide coordination modes. EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, 35(4), 340-351 [10.1007/s00249-005-0041-7].
Stellato, F; Menestrina, G; Dalla Serra, M; Potrich, C; Tomazzolli, R; Meyer Klaucke, W; Morante, S
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2108/39437
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