Bendazac prevents cyanate binding to soluble lens proteins and cyanate-induced phase-separation opacities in vitro: a possible mechanism by which bendazac could delay cataract.
The reaction of lens proteins with cyanate (carbamylation) causes many changes seen in human cataract including disruption of the protein conformations. Bendazac, a putative anti-cataract drug, decreases the binding of cyanate to lens proteins and prevents the cyanate-induced elevation of the phase separation temperature in incubated rat lenses. Its major metabolite, 5-hydroxybendazac, also inhibits the binding of cyanate to lens proteins even when it is present only during a pre-incubation period. The metabolite is more effective than the parent compound.
D000818:Animals; D001241:Aspirin / Q000494:pharmacology; D002417:Cattle; D003459:Crystallins / Q000378:metabolism*; D003485:Cyanates / Q000037:antagonists & inhibitors*; D007191:Indazoles / Q000494:pharmacology*; D011485:Protein Binding / Q000187:drug effects; D011720:Pyrazoles / Q000494:pharmacology*; D051381:Rats; D011919:Rats, Inbred Strains; D013696:Temperature
D003459:Crystallins; D003485:Cyanates; D007191:Indazoles; D011720:Pyrazoles; C051605:5-hydroxybendazac; C000123:bendazac; C024835:potassium cyanate; D001241:Aspirin