Human age-onset cataracts are a disease caused by the aggregation of gamma-D crystallin, a structural protein in the lens of the eye. The resulting aggregation causes progressive blindness. The purpose of this research is to determine the causes of these aggregates and their resulting structures. It is hypothesized that a hydrophobic core, five contiguous hydrophobic residues, is critical for the aggregation of gamma-D crystallin. Initial molecular dynamics simulations of small peptides containing a hydrophobic core of gamma-D crystallin were performed to examine possible aggregate structures.  Accurate structures of the aggregates will provide a basis for the long-term goal of designing drugs that will inhibit these aggregations to potentially prevent or treat cataracts.

Predicted structures of aggregates of the human gamma-D crystallin protein found in cataracts

245th National Meeting (2013)

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