Ali-Musa Jaffer

Mentor: Dr. Michael Bubb
College of Medicine
"My interest in research was cultivated by my penchant for neuroscience and statistical analyses. I wish to further my educational and career goals through the pursuit of research opportunities. Most important of all, research provides the foundation for growth - not only in the medical field, but in science as a whole."




Arabic Language and Literature

Research Interests

  • Alzheimer's Disease
  • Macromolecular Crowding
  • Protein Aggregation

Academic Awards

  • UF-HHMI Science For Life Intramural Undergraduate Research Award 2013-2014
  • University Scholars Program 2014-2015
  • UF Integration Bee Qualifier Spring 2013
  • Poster Presenter at UF-HHMI CASE Event – February 2014


  • Islam on Campus


  • Shands ED Hospital Volunteer
  • Project Downtown Food Service

Hobbies and Interests

  • Basketball
  • Arabic Grammar and Linguistics
  • Biking
  • Biking

Research Description

The Differential Effects of Macromolecular Crowding on Tau Aggregation and Interactions of Tau with Microtubules

In its natively unfolded form, tau is a natural protein that stabilizes tubulin polymerization into microtubules (MT), a key feature of the cytoskeleton. However, tau dissociates from MT and forms insoluble fibrils when abnormally phosphorylated, thus destabilizing the cytoskeleton. Phosphorylated tau (pTau) forms aggregates called paired helical filaments (PHFs), which are the principal constituents of neurofibrillary tangles - the pathological hallmarks of Alzheimer’s disease (AD). This research investigates the relationship between macromolecular crowding and the self-association of tau and interactions of tau with MT. “Crowding” refers to high volume occupancy by inert macromolecules. Due to high volume exclusion in these solutions, the system seeks chemical equilibrium by favoring changes that reduce the occupied volume. Two possible changes that can occur are protein folding and macromolecular association. It is hypothesized that crowding should accelerate aggregation over MT binding, since tau aggregation involves both protein folding and association, while tau-MT binding has been shown to possess only the latter. This study utilizes a pseudo-phosphorylated tau (7-phos) variant, which mimics the aggregation behavior of pTau. The results of this research can provide clues to the conditions required for tau pathology, which can provide mechanistic implications to Alzheimer’s disease pathology.