biostudies-literatureLermyte FBiotechnology and Biological Sciences Research CouncilEngineering and Physical Sciences Research Council2123-2134https://www.ebi.ac.uk/biostudies/studies/S-EPMC6805827biostudies-literatureUnknown30(10)Native top-down mass spectrometry is a fast, robust biophysical technique that can provide molecular-scale information on the interaction between proteins or peptides and ligands, including metal cations. Here we have analyzed complexes of the full-length amyloid β (1-42) monomer with a range of (patho)physiologically relevant metal cations using native Fourier transform ion cyclotron resonance mass spectrometry and three different fragmentation methods-collision-induced dissociation, electron capture dissociation, and infrared multiphoton dissociation-all yielding consistent results. Amyloid β is of particular interest as its oligomerization and aggregation are major events in the etiology of Alzheimer's disease, and it is known that interactions between the peptide and bioavailable metalJournal of the American Society for Mass SpectrometryMetal Ion Binding to the Amyloid β Monomer Studied by Native Top-Down FTICR Mass Spectrometry.PMC6805827EP/J000302/11679369BB/P021875/11745807EP/N033191/1BB/R022399/1EP/N021630/1EP/N033140/11837376Lermyte FEverett JBarrow MPLam YPYTelling NDSadler PJO'Connor PBCollingwood JFBrooks JWootton CAfalseMetal Ion Binding to the Amyloid β Monomer Studied by Native Top-Down FTICR Mass Spectrometry.Native top-down mass spectrometry is a fast, robust biophysical technique that can provide molecular-scale information on the interaction between proteins or peptides and ligands, including metal cations. Here we have analyzed complexes of the full-length amyloid β (1-42) monomer with a range of (patho)physiologically relevant metal cations using native Fourier transform ion cyclotron resonance mass spectrometry and three different fragmentation methods-collision-induced dissociation, electron capture dissociation, and infrared multiphoton dissociation-all yielding consistent results. Amyloid β is of particular interest as its oligomerization and aggregation are major events in the etiology of Alzheimer's disease, and it is known that interactions between the peptide and bioavailable metal2019-01-01T00:00:00Z2019 Oct2025-04-04T08:26:42.163Z2019-11-12T08:04:52ZS-EPMC68058273135072210.1007/s13361-019-02283-7