Author ORCID Identifier

https://orcid.org/0009-0001-5553-657X

Semester

Spring

Date of Graduation

2026

Document Type

Dissertation

Degree Type

PhD

College

Eberly College of Arts and Sciences

Department

Chemistry

Committee Chair

Lisa Holland

Committee Member

Stephen Valentine

Committee Member

Peng Li

Committee Member

Harry Finklea

Committee Member

Mariette Barbier

Abstract

Capillary electrophoresis as a tool for biomolecule analyses provides fast, high efficiency separations consuming only nanoliters of sample. Coupled to mass spectrometry, insight of analyte structure is gained which is not always easily determined by capillary electrophoresis alone. The work presented in the dissertation applies capillary electrophoresis – mass spectrometry coupled by a novel vibration based ionization source for the analysis of proteins, glycoproteins, and amyloids.

Protein detection with capillary electrophoresis is not straight forward. Positively charged analytes adsorb to the capillary and resolution between similarly charged large molecules can prove difficult. Capillary coatings were explored to both neutralize and change the charge of the capillary wall to increase the efficiency of the protein separations and expand the typical analyte set available when using a coated capillary. Vibrating sharp-edge spray ionization was also demonstrated the ionization of intact protein complexes.

Heterogeneous protein glycosylation can be incredibly difficult to characterize due to variation in glycan structure such as branching, sialylation, fucosylation, and the possibility of isomeric structures. Typically, glycans are cleaved from the protein and analyzed as a general population, however, that information is near impossible to piece back into a glycosylation profile of an intact glycoform. Here, nanoliter volume reactions were accomplished in-line during the separation to interact with or modify glycan structure for the elucidation the overall glycosylation of all detected glycoforms.

Since the outbreak of SARS-CoV-2, it has been reported that infection has resulted in the onset or acceleration of neurodegenerative disease. Amyloidogenic peptides of the SARS-CoV-2 Spike protein have been identified and reported to influence the aggregation of amyloid-β(1-42), a cause of Alzheimer’s diseases, as well as other aggregation prone proteins linked to neurodegeneration. Capillary electrophoresis – vibrating sharp-edge spray ionization – mass spectrometry was used to detect heteromeric aggregation between amyloid-β(1-42) and synthetic aglycosylated Spike protein amyloids.

Available for download on Wednesday, April 21, 2027

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