(188cj) Lanosterol Reverses Alpha-Crystallin Aggregates Induced By Different Denaturation Processes

Authors: 
Li, K. - Presenter, Missouri S&T
Forciniti, D., Missouri S&T
Lanosterol has been proven to have cataract restoration ability, but its mechanism is not well understood. Bovine lens alpha-crystallin aggregates, induced by heat, ultraviolet light, cold, denaturants (GdnHCl) and reactive oxygen species (ROS), were treated with lanosterol. Alpha-crystallin was also treated with lanosterol before undergoing the same denaturation process. All aggregation processes were monitored by thioflavin T (ThT) fluorescence assay, FT-IR and dynamic light scattering. Protein aggregates and restoration of aggregates were confirmed by transmission electron microscopy (TEM). Lanosterol affected the stability of the aggregates induced by all types of denaturation processes. The effect of lanosterol on the secondary structure of alpha-crystallin was investigated in detail by Fourier-transform infrared spectroscopy-attenuated total reflection (FTIR-ATR) and nuclear magnetic resonance (NMR), which show that lanosterol interacts with alpha-crystallin. DLS measurements suggest that the transition temperature of alpha-crystallin was decreased by the presence of lanosterol, which suggests that alpha-crystallin become more active at lower temperature. In summary, lanosterol reverses alpha-crystallin aggregates induced by all studied denaturation processes. This research advances our knowledge about the chaperon properties of lanosterol.