Amyloid fibrils are very stable, highly ordered protein aggregates that are characteristic of a large family of diseases, and their stability causes them to be dangerous. When proteins are damaged and misfold they can aggregate into amyloid fibrils. Cataracts are caused by the aggregation of proteins in the lens, specifically gammaD-crystallin, into aggregates proposed to be amyloid fibrils. It has been suggested that at least one of two hydrophobic cores, a sequence of five consecutive hydrophobic residues, is responsible for the nucleation of gammaD-crystallin aggregates. Molecular dynamics simulations were used to determine the propensity of aggregation of the hydrophobic core and its adjacent beta strand. Study of the aggregation of the truncated sequence of the protein was used to gain a greater understanding of protein folding and misfolding.

Mechanisms of aggregation in gammaD-crystallin

251st National Meeting (2016)

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