We previously identified an oxysterol， VP1-001 (also known as compound 29)， that partially restores the transparency of lenses with cataracts. To understand the mechanism of VP1-001， we tested the ability of its enantiomer， ent-VP1-001， to bind and stabilize αB-crystallin (cryAB) in vitro and to produce a similar therapeutic effect in cryAB(R120G) mutant and aged wild-type mice with cataracts. VP1-001 and ent-VP1-001 have identical physicochemical properties. These experiments are designed to critically evaluate whether stereoselective binding to cryAB is required for activity.
We previously identified an oxysterol， VP1-001 (also known as compound 29)， that partially restores the transparency of lenses with cataracts. To understand the mechanism of VP1-001， we tested the ability of its enantiomer， ent-VP1-001， to bind and stabilize αB-crystallin (cryAB) in vitro and to produce a similar therapeutic effect in cryAB(R120G) mutant and aged wild-type mice with cataracts. VP1-001 and ent-VP1-001 have identical physicochemical properties. These experiments are designed to critically evaluate whether stereoselective binding to cryAB is required for activity.
