32nd Annual Student Research Conference
Aggregation of Gamma S Crystallin
Lucy M. Gavlick
Dr. Cassidy Dobson, Faculty Mentor
Background:
Treatment of cataracts, the leading cause of blindness worldwide, may be improved with the development of a nonsurgical procedure. Intermolecular disulfide bonds between gamma crystallin proteins can result in aggregation, ultimately leading to cataracts. A chaperone protein called Disulfide Bond Forming Enzyme (DBF) shows promise in being able to rearrange incorrect disulfide bond formation and could be further applied to cataract treatment.
Methods:
Gamma S crystallin is isolated through recombinant protein expression and purification from E. coli. Aggregation of the protein over time was monitored by size exclusion chromatography (SEC) with fast protein liquid chromatography (FPLC) and visualized by SDS-PAGE.
Results:
Gamma S crystallin forms aggregates in as little as 2 weeks, with dimers present and possible larger aggregates.
Discussion:
Better understanding of the aggregation of gamma crystallins is crucial to moving on to the next step in research of studying how DBF may prevent or reverse aggregation.
Keywords: gamma crystallin, protein aggregation, fast protein liquid chromatography, size exclusion chromatography, SDS-PAGE
Topic(s):Chemistry
Biochemistry and Molecular Biology
Biology
Presentation Type: Poster
Session: 9-1
Location: SUB GEO
Time: 3:00