Abstract
Developing chemical strategies for selective labeling and functionalization of amino acids and post-translational modifications (PTMs) is of special interest in the realm of cell biology, pathogenesis, and therapeutic development. Access to these novel strategies will allow us to determine the biological functions associated with specific PTMs, through the discovery of novel proteomic sites, and can potentially lead to the discovery of biomarkers. Herein, we will first discuss the development of a novel pioneering chemical strategy that selectively labels 1-methyl histidine PTM, and its application for profiling novel sites in cell lysate. Additionally, strategies that incorporate unique functionality onto peptides are necessary for the development of new and improved therapeutics. Herein, we will also discuss a chemical strategy that installs a novel pyridinium scaffold onto lysine residues. This pyridinium has dual-functionality, containing fluorescent and organelle-targeting properties.
Table of Contents
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About this Dissertation
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