Abstract
This dissertation focuses on the study of interactions between transition metal ions [Cu(II), Zn(II), Pd(II), Pt(II)] and peptides (bradykinins and angiotensins). Chapter I provides an overview on the fundamental issues related to and techniques used for studying transition metal ion-peptide/protein complexes. It also reviews different mass spectroscopic techniques used for metal ion-peptide studies. Chapter II delineates the principle of 252Cf-PDMS instrumentation and the sample preparation methods utilized for this dissertation research. In order to study metal ion-peptide complexes with PDMS, it is essential to define the relationship between complex structures identified from PD mass spectra and complexes formed in solution phase. Chapter III includes the studies of the effects of solution conditions on the detection of metal ion-peptide complexes in PDMS. Solution pH is the most important factor for determining the formation of a complex. Reaction time, reactant concentration, and reaction temperature all display distinct influences on PDMS results. It demonstrates that the PDMS results are closely correlated with the complexes pre-formed in aqueous solution. Chapter IV provides ample spectroscopic data on peptides and their metal ion complexes. The metal ion-containing molecular ions observed provide information on numbers of metal ion-binding sites in a peptide and metal ion-affinity of the peptide. By analyzing fragmentation patterns, amino acid residues and functional groups involved in metal ion binding in a peptide can be identified.
Hu, Zhaohong (1993). Study of the interactions between transition metal ions and peptides by 252Cf plasma desorption mass spectrometry. Texas A&M University. Texas A&M University. Libraries. Available electronically from
https : / /hdl .handle .net /1969 .1 /DISSERTATIONS -1526994.