Stop The Swimmers! Inhibiting Flagellar EF-Hand Calcium Binding Domain Containing Protein 9
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Stop The Swimmers! Inhibiting Flagellar EF-Hand Calcium Binding Domain Containing Protein 9
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2022-12
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Sperm cells are a vital component of fertilization and maintain a complicated and multiplex anatomy that enables motility, survival, and protection for important genetic information. Following an extensive literature review, we identified a testis-specific protein that is advantageous for inhibition to produce reversible sterility in males without detrimentally impacting non-target tissues and cells. This protein, EF-hand CAlcium Binding Domain Containing Protein 9 (EFCAB9), is a major constituent of the flagellum in sperm cells. EFCAB9 is necessary for sperm cell mobility, motility, and controls the influx of calcium into the sperm flagellum to allow for hyperactivation and penetration of the ovum. EFCAB9 is an ideal target for reversible inhibition to cause temporary male sterility, because the protein expression pattern is localized in the testis and is vital for the systematic and intricate motion and hyperactivation of sperm cells. Molecular modeling and virtual docking software facilitates the structure-function-based drug design process to create small molecule inhibitors of the EFCAB9 protein. Additionally, miRNA silencing of the EFCAB9 mRNA strand prior to protein synthesis is explored as another method of inhibition. This work could lead to decreased sperm motility and male infertility that can be easily reversed. Ultimately, the development of male birth control will expand upon the currently-available options of condoms and vasectomies, and enhance individual sexual health and autonomy.
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Faculty Advisors: Cassidy R. Terrell & Rachel L.O. Olson
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This research was supported by the Undergraduate Research Opportunities Program (UROP).
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James, Alec G.; Terrell, Cassidy R.; Olson, Rachel L.O.. (2022). Stop The Swimmers! Inhibiting Flagellar EF-Hand Calcium Binding Domain Containing Protein 9. Retrieved from the University Digital Conservancy, https://hdl.handle.net/11299/250209.
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