Time- and pH-dependent copper binding to Aβ(1-16) peptide: An electrospray ionization-mass spectrometric approach

Marilena Manea, Gitta Schlosser, Manuela Murariu

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2 Citations (Scopus)


An elevated concentration of copper ions in the brain of Alzheimer's disease patients has been reported in many studies and might be associated with an increased aggregation of β-amyloid (Aβ) peptides. In the present work, the interaction with copper ions of a model β-amyloid peptide, Aβ(1-16), was investigated by electrospray ionization-mass spectrometry (ESI-MS) at two pH values, 7.4 and 6.6, as well as at various peptide: copper ion ratios in the first minutes after components mixing and time intervals. Our results indicated that copper ions specifically bound to Aβ(1-16) peptide in solution and that the complex formation increased with time. Once formed in solution, Cu2+-Aβ(1-16) complexes could easily be detected in the gas phase by ESI-MS. The pH shift from 7.4 to 6.6 only slightly influenced the Cu2+ binding to Ab(1-16). No oligomerization of Ab(1-16) peptide was noticed in the first minutes of copper-peptide interaction.

Original languageEnglish
Pages (from-to)125-131
Number of pages7
JournalInternational Journal of Peptide Research and Therapeutics
Issue number1
Publication statusPublished - Mar 2015



  • Alzheimer's disease
  • Copper-peptide complex
  • ESI-MS
  • pH
  • β-Amyloid peptide

ASJC Scopus subject areas

  • Analytical Chemistry
  • Bioengineering
  • Biochemistry
  • Molecular Medicine
  • Drug Discovery

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