Exploring the reactions of β-amyloid (Aβ) peptide 1-28 with Al(III) and Fe(III) ions.

Daniela Valensin, Caterina Migliorini, Gianni Valensin, Elena Gaggelli, Giovanni La Penna, Henryk Kozlowski, Chiara Gabbiani, Luigi Messori

Department of Chemistry, University of Siena, Via A. Moro, 53100 Siena, Italy. valensindan@unisi.it

Inorganic chemistry 2011 Aug 1

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The reactions of human β-amyloid peptide 1-28 (Aβ28) with Al(III) and Fe(III) ions were investigated by (1)H NMR and electrospray ionization mass spectrometry (ESI-MS) under pH conditions close to physiological ones. (1)H NMR titrations, performed in the 5.3-8.0 pH range, revealed that no measurable amounts of Aβ28-Al(III) or Aβ28-Fe(III) adducts are formed; such metal adducts could not be obtained even by changing a number of experimental conditions, e.g., temperature, buffer, nature of the salt, etc. These observations were later confirmed by ESI-MS. It is thus demonstrated that Aβ28, at physiological pH, is not able to form binary complexes with Al(III) and Fe(III) ions of sufficient stability to compete with metal hydroxide precipitation. The biological implications of these findings are discussed in the frame of current literature. © 2011 American Chemical Society

Citation

Daniela Valensin, Caterina Migliorini, Gianni Valensin, Elena Gaggelli, Giovanni La Penna, Henryk Kozlowski, Chiara Gabbiani, Luigi Messori. Exploring the reactions of β-amyloid (Aβ) peptide 1-28 with Al(III) and Fe(III) ions. Inorganic chemistry. 2011 Aug 1;50(15):6865-7