Office of Undergraduate Research

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Emphasizing equitable and inclusive access to research opportunities, the University of Maryland's Office of Undergraduate Research (OUR) empowers undergraduates and faculty to engage and succeed in inquiry, creative activity, and scholarship. This collection includes materials shared by undergraduate researchers during OUR events. It also encompasses materials from Undergraduate Research Day 2020, Undergraduate Research Day 2021, and Undergraduate Research Day 2022, which were organized by the Maryland Center for Undergraduate Research.

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    Recognition of Aminated Guests by Acyclic Cucurbiturils in Biological Conditions
    (2020) Shah, Rohan; Isaacs, Lyle; Zebaze, Sandra
    The acyclic cucurbituril Motor2 has already been well documented in its binding to several types of molecular guests in phosphate buffer. However, while these tests provide a rough idea of motor2 affinity to different types of guests, they are incomplete in that they do not reflect how motor2 actually binds in body conditions. The human body contains many proteins and macromolecules that can affect the host-guest interactions of motor2, so it is important for new binding constants to be measured for motor2 in body conditions. In order to do this, Isothermal Titration Calorimetry (ITC) was used to measure motor2 binding constants to several different guest types in several different solutions, including albumin and fetal bovine serum. It was found that when tested with cyclic, monoaminated guests, motor2 binding affinity did not decrease significantly from phosphate to protein serum solvents. This retained affinity held across several different ring sizes and shapes. Motor2 binding affinity did suffer greatly in protein serum for guests that were linear, regardless of how many amines they had. The results also indicated that more hydrophobic guests do not bind as well to motor2 once albumin and other proteins ae introduced to solution, while hydrophilic, polar guests have better affinity retention. The ITC testing results indicated that motor2 binding in body conditions is heavily dependent on the shape of the guests it is binding to, and that motor2 would be most effective at its purpose in the human body if it was used to target cyclic amines and similar types.
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    Inhibiting Degranulation in Immune Cell Signaling Pathways
    (2020) Fadul, Naja; Kasica, Zachary; Laurence, Kyeisha; Moy, Stephanie; Murugan, Sindhu; Pamala, Chinmayi; Robinson, Morgan; Shah, Rohan; Shrestha, Mansu; Smith, Marcus; Vashi, Bhavya; Frauwirth, Kenneth
    Allergies are a pervasive issue and require novel ways of alleviating symptoms. Existing treatments are focused on symptom management and immunotherapy, but there is also potential to target the molecules involved in the downstream pathway, particularly the PLCγ enzymatic pathway. Our research aimed to identify important target molecules involved in this pathway that result in the degranulation of mast cells. We intended to inhibit these molecules in order to hinder mast cell degranulation and therefore prevent allergic symptoms. Our results were tested and measured in MC/9 (mouse mast cell) and RBL-2H3 (rat basophilic) cell lines with multiple cell degranulation assays such as the beta-hexosaminidase and tryptase assay. The results were evaluated based on the comparative effect as well as specificity of inhibitors on mast cell degranulation. We aim to find the most ideal inhibitor for the PLCγ, SK, S1P2 enzymatic pathways in the signalling cascade in order to most effectively reduce degranulation and thus reduce the allergic response.