Glycosylation is a keystone of mammalian cells found primarily on membrane proteinsand lipids, extending into the extracellular space to form the outer-most membrane layer known as the glycocalyx. The physiological functions of glycans are still constantly being discovered in relation to specific glycan structures. These functions include alteration of protein tertiary structure, protection of the peptide backbone, and mediation of interactions. Each of these functionalities, namely the mediation of interactions, has been a recent focus in the field of glycomics. Glycans have been shown to play a significant role in signaling pathways, cancer pathology, neurodegeneration, immune response, and viral, bacterial, and fungal susceptibility pathology. Glycan-mediated interactions are of unique interest in neural physiology and pathology. Previous research has shown aberrant glycosylation of both proteins and lipids to play a significant role in neurological diseases such as multiple sclerosis, Huntington's disease, and Alzheimer's disease. The complexity of elucidating pathology mechanisms stems from the diversity of glycan structures specific to each cell type and how they shape interactions in vivo. Developing analytical methodologies that provide sensitive and reproducible profiles with structural information is critical to elucidate the mechanisms behind glycan interactions. The sheer structural diversity in glycans and their untemplated biosynthesis makes this challenging. The development of robust high-performance liquid chromatography-mass spectrometry workflows capable of generating structural profiles and their application was the primary focus presented in this work.