Protein aggregation in the eye often results in blindness due to opacification of the lens and cell death in the retina. In normal cells, small heat shock proteins (sHSP) are known to bind misfolded proteins and prevent aggregation and subsequent cell death. Our work focuses on harnessing these proteins to increase their levels in cells to prevent or delay protein aggregation. In previous studies, we identified a cell penetration peptide (CPP) that when fused to sHSP increases the cellular uptake of these proteins. These proteins are made using recombinant technique to produce large quantities of purified sHSP. These purified proteins have been studied using biochemical approaches and we have confirmed in vitro activities similar to unmodified sHSP. Moreover, these proteins when added to cells prevent cell death induced by heat or chemical stress. Ongoing work includes experiments to characterize mutations to the sHSP that affect their protective properties and to develop ways to improve bioavailability.
For a full list of publications from the laboratory, please click here.