Native Top-Down Mass Spectrometry and Ion Mobility MS for Characterizing the Cobalt and Manganese Metal Binding of α-Synuclein Protein
In: Journal of The American Society for Mass Spectrometry, Jg. 29 (2018-09-01), Heft 9
Online
academicJournal
- 1870 - 1880
Structural characterization of intrinsically disordered proteins (IDPs) has been a major challenge in the field of protein science due to limited capabilities to obtain full-length high-resolution structures. Native ESI-MS with top-down MS was utilized to obtain structural features of protein-ligand binding for the Parkinson's disease-related protein, α-synuclein (αSyn), which is natively unstructured. Binding of heavy metals has been implicated in the accelerated formation of αSyn aggregation. Using high-resolution Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometry, native top-down MS with various fragmentation methods, including electron capture dissociation (ECD), collisional activated dissociation (CAD), and multistage tandem MS (MS3), deduced the binding sites of cobalt and manganese to the C-terminal region of the protein. Ion mobility MS (IM-MS) revealed a collapse toward compacted states of αSyn upon metal binding. The combination of native top-down MS and IM-MS provides structural information of protein-ligand interactions for intrinsically disordered proteins. Graphical Abstract ᅟ.
Titel: |
Native Top-Down Mass Spectrometry and Ion Mobility MS for Characterizing the Cobalt and Manganese Metal Binding of α-Synuclein Protein
|
---|---|
Autor/in / Beteiligte Person: | Wongkongkathep, Piriya ; Han, Jong Yoon ; Choi, Tae Su ; Yin, Sheng ; Kim, Hugh I ; Loo, Joseph A |
Link: | |
Zeitschrift: | Journal of The American Society for Mass Spectrometry, Jg. 29 (2018-09-01), Heft 9 |
Veröffentlichung: | eScholarship, University of California, 2018 |
Medientyp: | academicJournal |
Umfang: | 1870 - 1880 |
Schlagwort: |
|
Sonstiges: |
|