Nonreciprocal XeCl laser-induced aggregation of beta-crystallins in water solution.

The aggregation of a beta-crystallin water solution exposed to XeCl laser radiation demonstrates the dependence of scattering-exposure curve (scattering versus exposure) on laser intensity. The main features of this dependence can be understood by the relaxation of a partly denaturated state of a protein within some finite relaxation time. These photoactivated states originate from the absorption of UV photons.

[Investigation of the mechanisms of crystallin aggregation induced by pulsed laser UV irradiation at 308 nm].

The results of the investigations of photoaggregation of the main eye lens proteins alpha-, beta- and gamma-crystallins and the model protein carbonic anhydrase in response to pulsed irradiation by a XeCI laser at 308 nm in the wide range of pulse energy densities (w) and pulse repetition rates (F) have been reviewed. A nonlinear dependence of aggregation efficiency on the values of w, F, and the concentration of protein solution was found. A theoretical model that qualitatively describes the experimental results was developed.

[Chaperon-like anticataract agents, the antiaggregants of lens crystallin. Communication 4. Study of the effect of a mixture of di- and tetrapeptides on a prolonged rat model of UV-induced cataract].

There is a potential of therapeutic action on certain stages of caractogenesis, in particular on the aggregation of water-soluble proteins of cytoplasmic lens fiber cells, giving rise to insoluble protein complexes. The effect of a combined preparation (N-acetyl carnosine and D-patethine), acting by the chaperon-like mechanism, was studied in vivo on a prolonged rat model of UV-induced cataract. The use of the combined preparation consisting of a mixture of peptides of N-acetyl carnosine and D-patethine in a ratio of 1:1 as ocular instillations and intraperitoneal injections could slow down the development of UV-induced cataract in vivo.

[Like anticataract agents, the antiaggregants of lens crystallin. Communication 2. Study of the impact of chaperon-like (protective) activity of short-chain peptides on the rate of UV-induced aggregation of betaL-crystallins by eximer laser].

UV-induced aggregation of betaL-crystallin, one of the major lens proteins, was studied under its pulse radiation with XeCl laser at a wavelength of 308 nm. Unlike the in vitro tested dipeptides L-carnosine, N-acetyl carnosine, D-panthetine, and particularly their combination, the so-called new chaperon was demonstrated to slow down the rate of photoaggregatin of beta-crystallin. The new chaperon, a mixture of D-pathethine and N-acetyl carnosine was ascertained to protect a mixture of betaL- and alpha-crystallins from UV-induced aggregation to a greater extent than D-pathethine or N-acetyl carnosine used alone.

Increased sensitivity of amino-arm truncated betaA3-crystallin to UV-light-induced photoaggregation.

Purpose: Exposure to UV-B light (wavelength, 290-320 nm) is a well-documented risk factor for age-related cataracts. As the lens ages, beta-crystallins tend to undergo proteolytic cleavage of their terminal extensions. To delineate the effects of loss of terminal arms on beta-crystallin function, the sensitivity of purified recombinant wild-type (rbetaA3) to UV-irradiation induced aggregation was compared with that of betaA3-crystallin missing the N-terminal extension (rbetaA3tr).