[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].

Autor: Soustov LV, Chelnokov EV, Sapogova NV, Bitiurin NM, Nemov VV, Karpova OE, Sheremet NL, Polunin GS, Avetisov SE, Ostrovskiĭ MA
Jazyk: ruština
Zdroj: Vestnik oftalmologii [Vestn Oftalmol] 2008 Mar-Apr; Vol. 124 (2), pp. 6-8.
Abstrakt: 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. An effective drug based on the new chaperon may be designed for the prevention of cataract in sight.
Databáze: MEDLINE