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dc.contributor.advisorVander Zanden, Crystal
dc.contributor.authorBrowne, Danielle Francine
dc.contributor.committeememberSemwal, Sudhanshu
dc.contributor.committeememberSackett, Robert
dc.date2020
dc.date.accessioned2020-08-15T20:49:02Z
dc.date.available2020-08-15T20:49:02Z
dc.description26 p.
dc.descriptionA Portfolio submitted to the Honors Program Faculty of the University of Colorado at Colorado Springs in partial fulfillment of the requirements for the UCCS Honors Program 2020.
dc.description.abstractLectin and glycolipid interactions are of emerging interest in biochemistry. These interactions take part in a vast array of cellular functions such as signaling, regulation, and adhesion which could serve as potential therapeutic tools for a variety of immune, inflammatory, and neurodegenerative diseases. Lectin and glycolipid interactions however are extremely complex and multidimensional, creating a challenge to isolate specific chains of cause and effect which are necessary to understand for potential medical use. As a part of the Vander Zanden research lab at UCCS, we have performed experiments to help elucidate the effects of wild type Gal-1, Gal-3NT/1, and the mutants Gal-1 [8S] Gal-1 to determine their interactions with glycolipid GM1. The goal was to investigate if the mutants with extended repeat domains produce different results than the wild type protein, with implications for improving our understanding of cellular functions. Experiments using Langmuir trough techniques, x-ray reflectivity (XR), and grazing incidence x-ray diffraction (GIXD) have allowed the elucidation of membrane structure and organization after the introduction of the galectin variants. Each of these experiments were done using a ratio of 80:20 DPPC lipid and ganglioside GM1 within the model membrane studied. These experiments combined with understanding of the sugar code presented along the surface of cellular membranes can help begin to unveil the function of the interactions between GM1 and Gal-1. However, there is much extensive future work still to be done before this research is able to be completed in a clinical setting due to the complexity of these signaling interactions, bringing our research to fruition. The complexity of interactions is the focus of the proposed research to understand cellular communication.
dc.identifier.urihttps://hdl.handle.net/10976/167619
dc.languageEnglish
dc.publisherUniversity of Colorado Colorado Springs, Kraemer Family Library
dc.relation.ispartofHonors Program Student Portfolios
dc.rightsCopyright of the original work is retained by the author.
dc.subjectBiochemistry Research
dc.titleDetermining the Effects of Galectin/GM1 Interaction on Cellular Membrane Structure and Organization
dc.typeText


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