Stoichiometry of Heavy Metal Binding to Peptides Involved in Alzheimer’s Disease: Mass Spectrometric Evidence

  • Monica Jureschi
  • Ancuta Veronica Lupaescu
  • Laura Ion
  • Brînduşa Alina Petre
  • Gabi DrochioiuEmail author
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 1140)


Mass spectrometry is a powerful analytical technique becoming increasingly important in different biomedical research area. Mass spectrometric based methods were developed and applied to detect and identify multiple metal ion complexes of peptides and proteins with high sensitivity and high mass accuracy. Aggregation of amyloid-β (Aβ) peptides is one of the main pathological features of Alzheimer’s disease (AD), and some metal ions seem to play a key role in AD pathogenesis. Consequently, mass spectrometry was used to investigate heavy metal binding to AD-related peptides. Therefore, the purpose of this chapter is to review the methodology and application of identifying coordination chemistry and binding properties of several metal ion-binding sites to synthetic β-amyloid (Aβ) and anti-amyloid model peptides. The selective metal–amyloid-β peptide interaction studies using (a) Matrix-assisted laser desorption/ionization mass spectrometry (MALDI); (b) Electrospray ionization mass spectrometry (ESI-MS), and (c) Tandem mass spectrometry (MS/MSn) will be reported.


Amyloid-β peptide Mass spectrometry Metal binding Neuroprotective peptide 



Alzheimer’s disease


Activity-dependent neurotrophic factor


Activity-dependent neurotrophic protein


Atomic force microscopy


Amyloid precursor protein

Beta-amyloid peptide


α-Cyano-4-hydroxycinnamic acid


Collision-induced dissociation


Dihydroxybenzoic acid


Electron capture dissociation


Electrospray ionization


Electron transfer dissociation


Extended X-ray absorption fine structure spectroscopy


Fourier-transform infrared spectroscopy


Liquid chromatography


Matrix-assisted laser desorption/ionization


Mass spectrometry


Tandem mass spectrometry


Neurofibrillary tangles


Nuclear magnetic resonance


Reactive oxygen species


Sinapinic acid


Scanning force microscopy




Tumor necrosis factor α


Time of flight



Funding from the Romanian Government (UEFISCDI Bucharest, PN-III-P4-ID-PCE-2016-0376, Contract 56/2017) is gratefully acknowledged by the authors.


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Copyright information

© Springer Nature Switzerland AG 2019

Authors and Affiliations

  • Monica Jureschi
    • 1
  • Ancuta Veronica Lupaescu
    • 1
  • Laura Ion
    • 1
  • Brînduşa Alina Petre
    • 1
    • 2
  • Gabi Drochioiu
    • 1
    Email author
  1. 1.Faculty of ChemistryAlexandru Ioan Cuza University of IasiIaşiRomania
  2. 2.Center for Fundamental Research and Experimental Development in Translation Medicine – TRANSCENDRegional Institute of OncologyIaşiRomania

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