This project focuses on characterizing the aggregates of a mutant Alpha 1-Antitrypsin protein associated with the disease Alpha 1-Antitrypsin Deficiency. Alpha 1-antitrypsin is a serine protease inhibitor that is crucial in the normal functioning of both the liver and the lungs. It protects the lung tissue from being damaged by proteases that work in the lung tissues to break down foreign invaders that cause infection. The protein contains 4 beta sheets that are hypothesized to be involved in the aggregation process. My goal is to characterize the structure of the monomers that make up the aggregates associated with the disease.<br/>Alpha 1-antitrypsin is expressed as a GFP fusion protein in the model organism, <i>C. elegans</i>. The proteins are extracted using a GFP affinity column; the GFP is cleaved after purification through the column. Size exclusion columns and native gels are being used to estimate the size of the mutant monomer; this will provide insight into whether the mutant forms a partially folded or completely unfolded protein that then forms aggregates.

Characterizing the aggregates of a mutant Alpha 1-Antitrypsin protein associated with Alpha 1-Antitrypsin Deficiency

249th National Meeting (2015)

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