Identifying the minimal Cu and Zn binding site sequence in amyloid beta peptides. (Articolo in rivista)

Type
Label
  • Identifying the minimal Cu and Zn binding site sequence in amyloid beta peptides. (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1074/jbc.M707109200 (literal)
Alternative label
  • Velia Minicozzi;? Francesco Stellato;? Massimiliano Comai;§ Mauro Dalla Serra;§ Cristina Potrich;§1 Wolfram Meyer-Klaucke;¶ and Silvia Morante;??2 (2008)
    Identifying the minimal Cu and Zn binding site sequence in amyloid beta peptides.
    in The Journal of biological chemistry (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Velia Minicozzi;? Francesco Stellato;? Massimiliano Comai;§ Mauro Dalla Serra;§ Cristina Potrich;§1 Wolfram Meyer-Klaucke;¶ and Silvia Morante;??2 (literal)
Pagina inizio
  • 10784 (literal)
Pagina fine
  • 10792 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 283 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 16 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • ?Dipartimento di Fisica, Universita` di Roma \"Tor Vergata\" and Istituto Nazionale di Fisica Nucleare, Via della Ricerca Scientifica 1, I-00133 Roma, Italy, the §Consiglio Nazionale delle Ricerche, Fondazione Bruno Kessler, Istituto di Biofisica, Unita` di Trento, Via alla Cascata 56/C, I-38100 Povo (TN), Italy, the ¶European Molecular Biology Laboratory, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany, and ?CRS-SOFT, c/o Dipartimento di Fisica, Universita` di Roma \"La Sapienza\", P.le A. Moro, 5, I-00185 Roma, Italy (literal)
Titolo
  • Identifying the minimal Cu and Zn binding site sequence in amyloid beta peptides. (literal)
Abstract
  • With a combination of complementary experimental techniques, namely sedimentation assay, Fourier transform infrared spectroscopy, and x-ray absorption spectroscopy, we are able to determine the atomic structure around the metal-binding site in samples where amyloid-beta (Abeta) peptides are complexed with either Cu(II) or Zn(II). Exploiting information obtained on a selected set of fragments of the Abeta peptide, we identify along the sequence the histidine residues coordinated to the metal in the various peptides we have studied (Abeta(1-40), Abeta(1-16), Abeta(1-28), Abeta(5-23), and Abeta(17-40)). Our data can be consistently interpreted assuming that all of the peptides encompassing the minimal 1-16 amino acidic sequence display a copper coordination mode that involves three histidines (His(6), His(13), and His(14)). In zinc-Abeta complexes, despite the fact that the metal coordination appears to be more sensitive to solution condition and shows a less rigid geometry around the binding site, a four-histidine coordination mode is seen to be preferred. Lacking a fourth histidine along the Abeta peptide sequence, this geometrical arrangement hints at a Zn(II)-promoted interpeptide aggregation mode. (literal)
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