An exploration of human γD-crystallin affinity for potential aggregation inhibitors: A molecular docking investigation

<p><span>These files contain the supplementary material to the article &ldquo;An exploration of human &gamma;D-crystallin affinity for potential aggregation inhibitors: A molecular docking investigation&rdquo; and the molecular docking simulation data.</span></p> <p><span>In this study, we performed a comparative molecular docking analysis of several experimentally investigated molecules of natural origin, that might protect &gamma;-crystallins from destabilization and aggregation. Our specific protein targets are wild-type human &gamma;D-crystallin, and its mutant P23T &gamma;D-crystallin, associated with congenital cataract. Thirteen phytochemicals were investigated as potential inhibitors of &gamma;D-crystallin aggregation, and we compared their binding energies with those of lanosterol, an ingredient present in over-the-counter eye products, to prevent cataracts. We performed a detailed comparative molecular docking analysis and we found that the binding energies of lanosterol outcompete those of all the other investigated potential natural inhibitors.</span></p>