Protein post-translational modification (PTM) crosstalk forms a complex regulatory program
within cells and mass spectrometry (MS) is a powerful tool to investigate this phenomenon.
Modification-specific studies using MS require efficient PTM enrichment tools. This thesis
will present the development and combination of enrichment strategies to characterise PTMs
with an emphasis on phosphorylation, glycosylation and lysine acetylation. Four publications
are presented utilising titanium dioxide (TiO2) to: 1) quantify N-linked glycoproteins during
extracellular matrix remodelling following acute myocardial infarction; 2) simultaneously
quantify phosphorylation and N-linked glycosylation during mouse brain development; 3)
simultaneously identify phosphorylation and O-linked N-acetylglucosmine (O-GlcNAc) sites
and; 4) simultaneously quantify phosphorylation and lysine acetylation during myocardial
ischemia and cardioprotection and, investigate intra- and inter-molecular crosstalk. The
development of these enrichment strategies and preliminary application to biological systems
represents a significant improvement to investigate PTM crosstalk.