Abstract 1364 Effects of Mutations on Bovine GammaB Crystallin Intermolecular Interactions

Cataracts formed from the aggregation of eye lens crystallin proteins affect millions of individuals worldwide. Many point mutations in crystallins have been linked to cataracts, and more needs to be understood as to the specific effects of these mutations on crystallin structure and intermolecular interactions. To elucidate the effects of mutations on bovine gamma-B crystallin (homolog to human gamma-D crystallin), we measured the cloud points of wild-type protein and its S130W, which is a useful metric for understanding protein stability and aggregation. The experiments revealed that the S130W mutant experiences decreased stability, opacifying at temperatures closer to that of the human body when compared to wild-type protein at similar concentrations. These findings will contribute to our understanding of the effects of mutations on crystallin protein stability and interaction, helping to bridge the current gap in our understanding of the many causes of cataracts. This work was supported by the Rochester Institute of Technology.