http://www.cnr.it/ontology/cnr/individuo/prodotto/ID168185
Metal binding in amyloid beta-peptides shows intra- and inter-peptide coordination modes (Articolo in rivista)
- Type
- Label
- Metal binding in amyloid beta-peptides shows intra- and inter-peptide coordination modes (Articolo in rivista) (literal)
- Anno
- 2006-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1007/s00249-005-0041-7 (literal)
- Alternative label
Stellato F., Menestrina G., Dalla Serra M., Potrich C., Tomazzolli R., Meyer-Klaucke W., Morante S. (2006)
Metal binding in amyloid beta-peptides shows intra- and inter-peptide coordination modes
in European biophysics journal
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Stellato F., Menestrina G., Dalla Serra M., Potrich C., Tomazzolli R., Meyer-Klaucke W., Morante S. (literal)
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- Univ Roma Tor Vergata, Dipartimento Fis, I-00133 Rome, Italy; INFM, I-00133 Rome, Italy; Ist Nazl Fis Nucl, I-00133 Rome, Italy; CNR, Ist Biofis, Sez Trento, I-38050 Povo, Italy; DESY, European Mol Biol Lab, D-22603 Hamburg, Germany (literal)
- Titolo
- Metal binding in amyloid beta-peptides shows intra- and inter-peptide coordination modes (literal)
- 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 Zn(2+) 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. (literal)
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