35th Annual Student Research Conference
Analysis of gamma-D Crystallin Aggregation in the Presence of Disulfide Bond-Forming Enzyme
Thomas J. Schodl
Dr. Cassidy Dobson, Faculty Mentor
Cataracts, a disease caused by the aggregation of gamma-crystallin in the lens of the eye, are the leading cause of blindness worldwide. This study sought to investigate if disulfide bond-forming enzyme (DBF) could mitigate or prevent the aggregation of gamma-D in vitro. Disulfide bond-forming enzyme has the ability to rearrange disulfide bonds and, unlike similar chaperones, contains no cysteine residues. To induce the aggregation of gamma-D the chemical oxidizing agent, oxidized glutathione was used. To produce aggregates of gamma-D, oxidized glutathione was used at different molar ratios to determine the best conditions for aggregation. This study laid a foundation for future aggregation studies by defining the molar ratio of oxidized glutathione needed to produce protein aggregates. Additional aggregations studies must be done to determine the effect of DBF. Some of these studies will include increasing the amount of DBF present in the reaction vial.
Keywords: Disulfide bond-forming enzyme (DBF), protein aggregation, gamma-D, gamma crystallin, biochemistry cataracts, oxidized glutathione
Topic(s):Biochemistry and Molecular Biology
Chemistry
Presentation Type: Poster Presentation
Session: 2-22
Location: SUB Activities Room
Time: 3:00