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.
Tipologia: | Articolo su rivista |
Citazione: | 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. |
Lingua: | English |
Settore Scientifico Disciplinare: | Settore FIS/07 - Fisica Applicata(Beni Culturali, Ambientali, Biol.e Medicin) |
Revisione (peer review): | Sì, ma tipo non specificato |
Tipo: | Articolo |
Rilevanza: | Rilevanza internazionale |
Digital Object Identifier (DOI): | http://dx.doi.org/10.1007/s00249-005-0041-7 |
Stato di pubblicazione: | Pubblicato |
Data di pubblicazione: | 2006 |
Titolo: | Metal binding in amyloid beta-peptides shows intra- and inter-peptide coordination modes |
Autori: | |
Autori: | Stellato, F; Menestrina, G; Dalla Serra, M; Potrich, C; Tomazzolli, R; Meyer Klaucke, W; Morante, S |
Appare nelle tipologie: | 01 - Articolo su rivista |