Graduate Research Assistant, College Of Medicine Molecular Medicine
14240 Monterey Pines Dr
Tampa, FL 33613
Academic Email: email@example.com
- BS, Biology, Morehouse College, 2011
Interdisciplinary and Emerging Signature Programs
- While chaperones are often linked to protein degradation, they also can preserve proteins. We have shown that one chaperone in particular, the constitutive Hsp70 variant, Hsc70, preserves free hyperphosphorylated tau, the accumulation of which can cause tauopathies including Alzheimer’s disease. In addition, other Hsp70 variants may be involved in the cell-to-cell propagation of tau; a recently discovered mechanism that could be contributing to the disease. Thus, inhibiting chaperones like Hsp70 proteins could be a novel therapeutic approach to treat multiple phases of tau diseases. To this end, we have screened a number of rhodacyanine derivatives designed to inhibit the Hsp70 family of chaperones for anti-tau activity. Our data shows that targeting Hsp70s may not only facilitate tau clearance inside of cells, but may also prevent its propagation in the brain.