Human ?D-crystallin is a structural protein in the lens of the eye that misfolds and aggregates to form cataracts. The purpose of this research is to determine if there is a critical part of the protein that can be targeted in drug design to prevent cataracts. It is hypothesized that a hydrophobic core of five contiguous hydrophobic residues is critical for aggregation, as seen with the human amyloid-beta protein. Molecular dynamic simulations of small peptides containing the hydrophobic core of ?D-crystallin were performed to determine if one of the two hydrophobic cores present in full-length ?D-crystallin is critical for aggregation. The structure of these aggregates and the mechanism by which they form was also examined.

Molecular dynamics simulations of human ?D-crystallin aggregates found in cataracts

247th National Meeting (2014)

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