Valerio Rasi

Mentor: Dr. Robert McKenna
College of Medicine
 
"After two years of college, I felt that I needed to explore science from a different perspective than classroom or teaching lab. Research has allowed me to use science as a tool to develop strategies that would sustain and improve patient care. My plan is to attend medical school and become a physician that also devolves time and energies into research. "

Major

Interdisciplinary Studies in Biochemistry and Molecular Biology

Minor

History

Research Interests

  • Carbonic Anhydrase
  • Over-expressed tumors
  • Biophysical approach on enzymes

Academic Awards

  • President Honor Roll
  • Dean's list
  • Provost Honor Roll

Organizations

  • Florida Club Swimming and Diving
  • P3 mentoring Program

Volunteer

  • North Florida ER Patient Ambassador
  • Shands ER
  • Shands Radiology

Hobbies and Interests

  • Swimming
  • House MD
  • House of Cards
  • Travel

Research Description

Characterization of the ā€œ230sā€ loop of CAIX and CAXII, Tumor Associated Enzymes
Cells that express the extracellular transmembrane proteins carbonic anhydrase isoforms IX and XII (CAIX and XII) are associated with highly aggressive tumor proliferation. The optimal catalytic pH for these proteins is 6.5 and 8.0 for CAIX and CAXII, respectively. We hypothesize this pH difference is due to the amino acid sequence variation in a loop (residues 230-240, termed the 230s loop) adjacent to the active site, which may significantly modify the active site pKs and therefore catalytic activity (Fig.1). Both kinetic and X-ray crystallography studies will be performed to help understand the role of this loop using CAII loop variants that mimic the 230s loop of CA IX and CA XII. Results could lead to the design of a drug inhibitor that binds more tightly to the enzyme's active site.