Copper(II) complexation to 1-octarepeat peptide from a prion protein: Insights from theoretical and experimental UV-visible studies

The octarepeat domain in cellular prion protein (PrPC) has attracted much attention over the last 10 years because of its importance in the complexation of copper with PrPC. The aim of this research was to study the UV–vis spectra of a peptide similar to the 1-repeat of the octarepeat region in PrPC using experimental and theoretical approaches and to gain insight into the complexation of the PrPC octarepeat domain with copper(II) ions in solution. We found that the copper atom was responsible for the peptide conformation, which allows for charge transfers between its two terminal residues.

Copper atom was responsible for the peptide structure, which allows for charge transfers between its two terminal residues.Figure optionsDownload as PowerPoint slideHighlights
► The experimental and theoretical spectra confirm the spiral structure assumed by the peptide.
► The copper atom is responsible for the structure assumed by the peptide.
► The copper atom allows the charge transfer between the two peptide terminal residues.
► This spiral structure could be replicated to determine the octarepeat structure of PrPC.