{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lermyte F"],"funding":["Biotechnology and Biological Sciences Research Council","Engineering and Physical Sciences Research Council"],"pagination":["2123-2134"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6805827"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["30(10)"],"pubmed_abstract":["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 metal"],"journal":["Journal of the American Society for Mass Spectrometry"],"pubmed_title":["Metal Ion Binding to the Amyloid β Monomer Studied by Native Top-Down FTICR Mass Spectrometry."],"pmcid":["PMC6805827"],"funding_grant_id":["EP/J000302/1","1679369","BB/P021875/1","1745807","EP/N033191/1","BB/R022399/1","EP/N021630/1","EP/N033140/1","1837376"],"pubmed_authors":["Lermyte F","Everett J","Barrow MP","Lam YPY","Telling ND","Sadler PJ","O'Connor PB","Collingwood JF","Brooks J","Wootton CA"],"additional_accession":[]},"is_claimable":false,"name":"Metal Ion Binding to the Amyloid β Monomer Studied by Native Top-Down FTICR Mass Spectrometry.","description":"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 metal","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Oct","modification":"2025-04-04T08:26:42.163Z","creation":"2019-11-12T08:04:52Z"},"accession":"S-EPMC6805827","cross_references":{"pubmed":["31350722"],"doi":["10.1007/s13361-019-02283-7"]}}