Short-chain peptides as a promising class of chaperone-like anticataract agents: Molecular mechanism of inhibition of crystallin aggregation by pantethine

Abstract

The molecular mechanism of inhibition of UV-induced aggregation of a mixture of gA and gBL-crystallins in the presence of pantethine, a representative of a new promising class of chap-erone-like anticataract agents, was studied in vitro. Pantethine (5–25 mmol L-1) enhances the chaperone-like properties of gA-crystallin and also functions as an UV filter by decreasing the amount of UV light falling on gBL-crystallin. Using a fluorescence probe, 1,1’-bis(4-anilino-naphthalene-5-sulfonic acid), it was found that pantethine considerably increases the number of binding sites for hydrophobic substrates on the gA-crystallin molecule. By dynamic light scattering, it was shown that the presence of pantethine increases the size of the gA-crystallin molecule.