Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7755592 | Journal of Inorganic Biochemistry | 2012 | 8 Pages |
Abstract
⺠The peptide with three histidyl residues HuPrP(84-114) can simultaneously bind two equivalents of copper(II) and one equivalent of nickel(II) ions. ⺠H85 and H111 were identified as the major copper(II) and H96 as the preferred nickel(II) binding sites. ⺠The data provide further support for the outstanding affinity of copper(II) ions towards the peptide fragments of prion protein. ⺠Binding of nickel(II) can significantly modify the distribution of copper(II) among the available metal binding sites.
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
Authors
Viktória Jószai, Ildikó Turi, Csilla Kállay, Giuseppe Pappalardo, Giuseppe Di Natale, Enrico Rizzarelli, Imre Sóvágó,