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DTSTART;TZID="Pacific Time (US & Canada)":20260424T130000
DTEND;TZID="Pacific Time (US & Canada)":20260424T140000
SUMMARY:Chemistry Final Defense – Eric Jacobo
LOCATION:Fulmer Hall
DESCRIPTION:Speaker: Eric Jacobo\n\nGroup: Dr. Jim Brozik\n\nTitle: Developing Single-Molecule Fluorescence Methods for Measuring Kinetic and Thermodynamic Properties Essential for Aquaporin-4 Function and Regulation\n\nAbstract: Aquaporin-4 (AQP4) is a water channel protein located at the end feet of astrocytes in the central nervous system (CNS), where it regulates water homeostasis. AQP4 is an important transmembrane protein involved in numerous regulatory functions, including self-regulation and interactions with the dystrophin-associated protein complex (DAP). AQP4 has two isoforms, M1 and M23, which differ in the length of their N-terminus; M1 starts at the first methionine (long form), while M23 begins at the twenty-third methionine (short). The M23 isoform forms an orthogonal array of proteins (OAPs), whereas M1 forms a cap around these arrays. The exact mechanism by which AQP4-M23 forms OAPs remains largely unknown, but it is believed to involve hydrogen bonding between helices 3 and 8 of AQP4. These OAPs are involved in normal functions supporting learning and memory, and disruptions in OAP localization have been linked to Alzheimer's disease and other CNS disorders. Additionally, AQP4 OAPs interact with the DAP at the blood-brain barrier through the extended region at the C-terminus. It has been shown that AQP4 OAPs are crucial for stabilizing the DAP through direct interaction with α-syntrophin. However, the specific details of these interactions, the forces driving OAP formation, and the binding mechanisms with α-syntrophin remain incompletely understood. In this study, single-molecule imaging and tracking are used to observe interactions between synthesized peptides and the proteins of AQP4-M23 and α-syntrophin. This direct observation approach has allowed the determination of the thermodynamic forces between the AQP4 extended region and α-syntrophin, as well as the specific  amino acid interactions behind AQP4 self-assembly.
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