Study of the Metal Ions Binding Behavior of Methanobactin Analog Peptides by Traveling Wave Ion Mobility Mass Spectrometry
Master of Science (MS)
Date of Award
The research investigates the metal ion binding behavior of an analog methanobactin (amb) peptide with the sequence acetyl-His1-Cys2-Gly3-Ser4-Try5-Pro6-His7-Cys8-Ser9 using electrospray ionization - ion mobility - mass spectrometry (ESI-IM-MS) and compares it to the binding of the non-acetylated His1-Cys2-Gly3-Ser4-Try5-Pro6-His7-Cys8-Ser9 peptide. Survey scans with a series of divalent 3rd row transition metal ions showed both ambs bound specifically to Zn(II), Cu(II), Cu(I) and Ni(II) and binding was pH dependent. In this work the main focus is to measure the pH dependent metal ion binding behavior of CuI/II), Zn(II) and Ni(II), and measure their collision cross section (A2 ) from the drift time measurements. Using α,ω-dicarboxy-terminated polystyrene oligomer as calibrants, the collision cross section of the various negative charged species will be determined. Selected charge states of angiontensin I and angiotensin II will be used as calibrants for positive ions. Cross section measurement give information on the shape and size of the structural conformations of the peptide complexes .
Laurence A. Angel
Chemistry | Physical Sciences and Mathematics
Alshehri, Hind Rafie, "Study of the Metal Ions Binding Behavior of Methanobactin Analog Peptides by Traveling Wave Ion Mobility Mass Spectrometry" (2014). Electronic Theses & Dissertations. 556.