Many diseases are a result of protein aggregation, which occurs when the protein is damaged and subsequently misfolds and aggregates. Cataracts are formed by damage to the proteins that compose the lens of the eye, specifically γD-crystallin. Molecular dynamics simulations were performed to determine if one of the hydrophobic cores, a contiguous section of five or more hydrophobic residues, within γD-crystallin is critical for aggregation. Determining the propensity for aggregation of this hydrophobic core might be used to design a drug that can prevent or treat cataracts. The aggregation methods exhibited with these small peptides were also examined and mechanism(s) for aggregation between γD-crystallin peptides containing a hydrophobic core will be described.

Nucleation mechanisms of γD-crystallin protein aggregates found in cataracts

249th National Meeting (2015)

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