Chaperoned Aggregation of Gamma D Crystallin Proteins
Gamma D crystallin is a human protein commonly found in the human eye. The aggregation of which is a leading cause of cataracts. This work focuses on the optimization of aggregation conditions for gamma D crystallin in order to investigate the effect of molecular chaperones on the reversal and prevention of the aggregation. By optimizing the aggregation conditions a reliable production of gamma D crystallin aggregate can be achieved. This work focuses on varying the incubation time of gamma D with chemical oxidizers to induce aggregation with and without the presence of a molecular chaperone (DBF). Results were analyzed through the use of SDS PAGE. We were able to determine the effect of varying incubation times of gamma D aggregation. Future work will focus on optimizing other aggregation conditions such as molar ratios and the presence of other gamma crystallin proteins.
Keywords: gamma crystallins, SDS PAGE, protein aggregation, DBF, molecular chaperone
Topic(s):Chemistry
Biochemistry and Molecular Biology
Presentation Type: Oral Presentation
Session: 205-1
Location: MG 2001
Time: 10:15