35th Annual Student Research Conference
Optimizing the Aggregation of Gamma S Crystallin
Samantha A. Webster
Dr. Cassidy Dobson, Faculty Mentor
Gamma crystallins are the proteins whose aggregation is responsible for the formation of cataracts in the eye lens. Disulfide Bond-Forming enzyme (DBF) has been identified as a known disulfide protein chaperone and can be used to refold a variety of proteins. DBF has the possibility to correct or even potentially reverse the protein folding, leading to cataracts. In order to test this, more information needs to be obtained in regard to the conditions under which Gamma crystallins aggregate. This research focuses on the optimization of the aggregation conditions of the Gamma S crystallin by studying the cystallin in vitro, looking at various variables, such as the identity of the oxidizing agent, the optimal ratio of protein to oxidant, and the time of the incubation. These conditions were tested using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Future work can be done to look at how DBF can affect gamma crystallin aggregates to prevent or reverse cataracts and if this changes based on the aggregation conditions of Gamma S crystallin.
Keywords: gamma crystallins, aggregation, Gamma S, oxidizing agent, DBF
Topic(s):Biochemistry and Molecular Biology
Presentation Type: Asynchronous Virtual Presentation
Session: 3-4
Location: https://flipgrid.com/d54e4a1e
Time: 0:00