Article ID Journal Published Year Pages File Type
7755592 Journal of Inorganic Biochemistry 2012 8 Pages PDF
Abstract
► The peptide with three histidyl residues HuPrP(84-114) can simultaneously bind two equivalents of copper(II) and one equivalent of nickel(II) ions. ► H85 and H111 were identified as the major copper(II) and H96 as the preferred nickel(II) binding sites. ► The data provide further support for the outstanding affinity of copper(II) ions towards the peptide fragments of prion protein. ► 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
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