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

J Inorg Biochem. 2012 Sep:114:1-7. doi: 10.1016/j.jinorgbio.2012.04.008. Epub 2012 Apr 27.

Abstract

The octarepeat domain in cellular prion protein (PrP(C)) has attracted much attention over the last 10 years because of its importance in the complexation of copper with PrP(C). 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 PrP(C) using experimental and theoretical approaches and to gain insight into the complexation of the PrP(C) 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Cations, Divalent
  • Coordination Complexes / chemistry*
  • Copper / chemistry*
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Peptide Fragments / chemical synthesis*
  • Peptide Fragments / chemistry
  • PrPC Proteins / chemistry*
  • Protein Binding
  • Protein Structure, Tertiary
  • Repetitive Sequences, Amino Acid
  • Spectrum Analysis
  • Static Electricity

Substances

  • Cations, Divalent
  • Coordination Complexes
  • Peptide Fragments
  • PrPC Proteins
  • Copper