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Author ORCID Identifier


Open Access Dissertation

Document Type


Degree Name

Doctor of Philosophy (PhD)

Degree Program


Year Degree Awarded


Month Degree Awarded


First Advisor

Richard W. Vachet

Subject Categories

Life Sciences


Protein post-translational modifications (PTMs) play key roles in cellular physiology and disease, and identifying their locations on proteins can be beneficial for understanding more deeply protein chemistry. The methods applied for PTM analysis are most often based on mass spectrometry (MS). In the past few years, considerable progress has been made in developing MS-based proteomics technologies for global PTM analysis. Novel mass spectrometric peptide sequencing and analysis technologies allow for modification site mapping at molecular level. However, detecting PTMs on proteins and peptides by MS is challenging because of their low abundance and heterogeneity. Therefore, separation prior to MS analysis is typically required. This dissertation describes the use of supramolecular nanoassemblies, formed by amphiphilic polymers, as novel enrichment tools for the detection and analysis of peptides and proteins that are phosphorylated and glycosylated. The selectivity of the amphiphilic nanoassemblies were changed by loading metal ions for the enrichment of phosphopeptides and by incorporating hydrazide functional groups for the enrichment of glycopeptides. In addition to developing new nanoassemblies for the enrichment of phosphopeptides and glycopeptides, we also explored how supramolecular systems could be tuned to enhance extraction selectivity and efficiency via structural variations to the amphiphilic polymers. The utility of these materials for the enrichment of phosphopeptides and glycopeptides from complexed samples is also demonstrated.


Included in

Life Sciences Commons