"I applied to the University Scholars program because I was interested in conducting my own research project under the supervision of a mentor. I found this program to be ideal because it gives one the opporutnity to do research in whatever area one holds interest and also it gives one a lot of flexibility to manage your own project at your own pace. My goals for this year are to finish collecting all the data necessary to arrive at a significant conclusion and hopefully write a paper to be published in a science journal."
Biochemical mechanisms underlying neurological disorders.
Academic and Other Awards
- University Scholars Program Scholarship (2011-2012)
- Florida Medallion Scholars
- National Society of Collegiate Scholars
- Children Beyond our Borders (SMDEP)
Shands Volunteer Crossing Borders service trip.
Hobbies and Interests
Effects of Methionine Substitution at the Alpha Helix-3 on Structure and Function of the Prion Protein
Prion disorders are neurodegenerative disorders associated to the misfolding of prion protein (PrPC) into a pathogenic conformation. The normal prion protein is a soluble membrane-anchored glycoprotein that contains three α-helices and two β-pleated domains. During disease the globular domain misfolds and its β-sheet content increases, leading to the aggregation of abornal prion protein conformations. Although, scientists know that this accumulation leads to tissue damage and cell death, what governs the conformational change of cellular PrP is a mystery yet to be solved. The laboratory of Dr. Fernandez-Funez uses the fruit fly Drosophila to study PrP misfolding and neurotoxicity. Previous experiments using this model have demonstrated that small alterations in the PrP sequence have dramatic effects on the structural stability of PrP. Furthermore, my project aims to look at the effect of methionine-to-serine substitution at position 206 and 213 on the stability and post-translational modificaions of PrP. The methionines at these two specific sites are known to be very well conserved in most species and also to form key hydrophobic interactions between alpaha helix-1 and helix-3 two factors that if disturbed can potentially lead to similar effects seen with the pathogenic form of cellular PrP. Through different biochemical assays, viability and locomotor assays I plan to evaluate wheather these substituions increase the structural instability of PrP, therefore result in heightened neurotoxicity. If this replacement proves to have significant effects on neurodevelopmental impairment and toxicity, these findings would provide the basis to perform screens to possibly identify genetic supressor, a poorly understood area of prion bioloy.