Aggregation of crystallins induced by pulsed laser UV light (308 nm)

Abstract

Here we compile and analyze the data on photoaggregation of a model protein carboanhydrase and the main eye lens proteins α-, β-, γ-crystallins under the action of pulsed UV irradiation from a Xe-Cl laser (308 nm) with broad variation of pulse energy density and repetition rate. The aggregation efficacy proves to be a nonlinear function of these parameters and protein concentration. A theoretical model is proposed that qualitatively explains the experimental data. It is shown that N-arm-truncated βA3-crystallin is more prone to UV-induced aggregation than the full-sized protein; such defects caused by mutation or aging may aggravate the development of lenticular opacity. Analyzed is the effect of some low-molecular compounds on the aggregation of β-crystallin and its mixture with α-crystallin. A combination of short peptides prepared on this basis markedly impedes crystallin aggregation and retards the development of UV-induced cataract in rats.