Title
The pH Dependent Study of Zinc(II), Nickel(II) and Copper(II) Binding by Histidine Motif Heptapeptides Using ESI-IMMS
Document Type
Thesis
Degree Name
Master of Science (MS)
Department
Chemistry
Date of Award
Fall 2021
Abstract
Metals are useful in fixing the health physiology of the body by direct administration as well as carriers for targeted drug deliver. Copper is an important metal in the nervous system development, when its homeostasis is disrupted, there is neurodegenerative disorder. A series of four structurally related heptapeptides Amb5O-R were investigated with ion mobility-mass spectrometry (IM-MS) to compare the binding nature and to probe each of these heptapeptides amb5O:ac-His1-His2-Gly3-Pro4-Tyr5-His6-His7,amb5P:ac-His1-His2-His3-His4-His5-His6-His7,amb5Q:ac-His1-His2-His3-Pro4-His5-His6-His7 and amb5R:ac-His1-His2-Gly3-Pro4-Gly5His6-His7 binds with Cu(II), Ni(II) and Zn(II) under different pH condition from pH 7.0-9.0 as a new discovery for potential affinity tags. The research also investigated the effect of tyrosine amino acid to that of proline and the polyhistidine sequence on the binding ability of these peptides with metal ions. Collision induced dissociation (CID) was used to analyze the fragmentation energies of the complexes and the influence of hydrophilic hydroxyl group on tyrosine and histidine relative to fragmentation of parent ion.
Advisor
Laurence A. Angel
Subject Categories
Chemistry | Physical Sciences and Mathematics
Recommended Citation
Falokun, Oladapo S., "The pH Dependent Study of Zinc(II), Nickel(II) and Copper(II) Binding by Histidine Motif Heptapeptides Using ESI-IMMS" (2021). Electronic Theses & Dissertations. 530.
https://digitalcommons.tamuc.edu/etd/530
