Arianna Cook

Mentor: Dr. Ben MDunn
College of Medicine
"My curiosity about the human body developed my interest in food science and human nutrition. Like medicine, research is an integral part of food science that leads to the creation of novel food and crops. Instead of just learning about the research conducted by others, I wanted my own research experience outside of the classroom. I began working under Dr. Dunn in the Department of Biochemistry and Molecular Biology to continue to learn about the impact of diseases on the body and gain insight into the work behind developing pharmaceutical drugs. "


Food Science


Nutritional Sciences and Classical Studies

Research Interests

  • Human Disease
  • Drug Development

Academic Awards

  • Eugene Chester Terzenbach Memorial Scholarship
  • Anderson Scholar


  • Delta Zeta


  • UF Health Shands Hospital
  • P.K. Yonge Developmental Research School

Hobbies and Interests

  • Soccer
  • Cooking

Research Description

Truncation and Expression of Aspartic Acid Protease Plasmepsin 10

Malaria kills around 700,000 people each year, most of them being children. Although there are drug treatments available, the immunity to these drugs has increased due to rapid rates of mutation and has created an immediate need for new medication. My project focuses on Plasmepsin 10 (PM 10) because it could be a potential drug target against the parasite. Plasmepsins are aspartic acids proteases found in the malaria parasite and are involved in the degradation of hemoglobin during the erythrocyte stage. PM 10 is found outside of the parasite’s digestive vacuole and is present in an infected red blood cell, indicating that PM 10 may be vital to the plasmodium life cycle. The expression of PM 10 will be performed through Escherichia coli cells, which will allow for the collection of active protein. The success of expression will allow for the collection of inclusion bodies through the purification process. Active recombinant protein will be acquired through solubilization and refolding and tested for activity through enzyme kinetics. Protein crystallization will be obtained based on crystal optimization trays and the resulting protein structure will be utilized to create specific inhibitors targeting PM 10.