Ziqi Wang

Mentor: Dr. Todd Golde

College of Medicine

"I initially became involved with research as a result of my fascination with how the human body acts as a system and the ways in which this system can go awry. I stayed on with research because I gradually fell in love with the intricate experiments and rigorous scientific reasoning, as well as the fact that the research done today has the potential to benefit future generations of patients. My experience in the Golde Lab has demonstrated to me the translational aspects of research and piqued my interest in neuroscience research. I believe that the research experiences I will have garnered as an undergraduate student will be instrumental in my future career as a physician and clinical scientist."

Major

Biochemistry

Minor

N/A

Research Interests

  • Neurodegeneration
  • Alzheimer's Disease
  • Neuroimmunology

Academic Awards

  • Stamps Leadership Scholar (2015)
  • Hazen E. Nutter Scholarship (2016)
  • Savant Outstanding First Year Leadership Award (2016)
  • University Scholars Program (2017-2018)

Organizations

  • UF Impact Autism
  • Prism: the UF Honors Magazine

Volunteer

  • UF Shands Arts in Medicine
  • UF Impact Autism

Hobbies and Interests

  • Art and Illustration
  • Reading
  • Crossword Puzzles
  • Running, Cycling, Swimming

Research Description

Using Functionalized Intrabodies to Target Tau Protein to the Lysosome for Degradation
Recent publications have demonstrated the potential of intracellular antibody fragments (intrabodies) as novel therapies to treat neurodegenerative diseases by binding to pathological protein aggregates within the cell. Intrabodies specific for tau (a protein that forms the characteristic neurofibrillary tangles in Alzheimer's Disease and other forms of neurodegeneration) have been developed and shown to be efficacious in mouse models of tauopathy. However, the efficacy of these intrabodies may be improved by adding functional domains using molecular cloning techniques. The hypothesis is that fusion of a lysosomal targeting sequence onto an anti-tau intrabody will be able to target tau to the lysosome for degradation, thus reducing insoluble tau levels within the cell. Molecular cloning will be used to fuse the lysosomal targeting sequences with intrabodies specific for phosphorylated tau. The new intrabody constructs will be ligated into a plasmid and expressed by transfection in HEK-293T cells. They will then be tested in a tau seeding assay to determine if they are more effective at reducing insoluble tau than the intrabodies lacking the lysosomal targeting sequences (the controls). The ability of the intrabody construct to alter tau protein levels will be evaluated by harvesting the cells and conducting immunoblotting assays for phosphorylated and total tau protein levels. The intrabody constructs will also be tested on primary neuronal culture in order to further analyze the ability of the intrabody constructs to degrade insoluble tau protein in vitro.