35th Annual Student Research Conference
Determination of the Impact of Copper(II) chloride on DBF as a Molecular Chaperone for Gamma Crystallin D
Sutton Q. Purinton
Dr. Cassidy Dobson, Faculty Mentor
Similar to other infamous diseases such as Alzheimer’s Disease, protein aggregation is also to blame for blindness. Cataracts, the leading global cause of blindness, are the direct result of gamma crystallin proteins aggregating. These gamma crystallin aggregates often contain intermolecular disulfide bonds making it difficult to reverse any aggregation. Disulfide bond forming enzyme (DBF) has great potential as a molecular chaperone due to its lack of cysteine residues which aid in its ability to reverse improper disulfide formation. In this experiment, the impact of DBF on oxidized and unoxidized gamma crystallin D aggregation was studied using Copper(II) chloride (CuCl2), a known oxidizing agent responsible for disulfide formation. Observing how CuCl2 causes gamma crystallin D to aggregate and how DBF functions in the presence and absence of CuCl2 will answer if CuCl2 is the best oxidizing agent for gamma crystallin D as well as answer if DBF is as effective of a chaperone for oxidized gamma crystallin D as it was for unoxidized gamma crystallin D.
Keywords:
Topic(s):Biochemistry and Molecular Biology
Chemistry
Presentation Type: Asynchronous Virtual Presentation
Session: 3-6
Location: https://flipgrid.com/d54e4a1e
Time: 0:00