Off-campus UMass Amherst users: To download campus access dissertations, please use the following link to log into our proxy server with your UMass Amherst user name and password.

Non-UMass Amherst users: Please talk to your librarian about requesting this dissertation through interlibrary loan.

Dissertations that have an embargo placed on them will not be available to anyone until the embargo expires.

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

Second Advisor

S. Thayumanavan

Subject Categories

Amino Acids, Peptides, and Proteins | Analytical Chemistry | Biomedical and Dental Materials | Investigative Techniques | Materials Chemistry | Organic Chemistry | Other Analytical, Diagnostic and Therapeutic Techniques and Equipment | Other Biochemistry, Biophysics, and Structural Biology | Polymer Chemistry


Mass spectrometry (MS) has played an increasingly prominent role in proteomics and structure biology because it shows superior capabilities in identification, quantification and structural characterization of proteins. To realize its full potential in protein analysis, significant progress has been made in developing innovative techniques and reagents that can couple to MS detection. This dissertation demonstrates the use of polymeric supramolecular assemblies for enhanced protein detection in complex biological mixtures by MS. An amphiphilic random co-polymer scaffold is developed to form functional supramolecular assemblies for protein/ peptide enrichment. The influences of charge density and functional group pKa on host-guest interactions within the assemblies are fundamentally investigated. In practice, these new materials enable specific isolation of target peptides from complex mixtures, as well as enhance MS detection/ quantification of protein biomarker in human breast milk. In parallel to protein detection, this dissertation also describes the development of a series of small-molecule covalent labeling (CL) reagents that are capable of studying protein higher order structure and protein-protein interactions when coupled with MS.