Preferential hydrolysis of kynurenine peptides.

The preferential cleavage of kynurenine peptides bonds was studied through reduction to y-(oaminophenyl)-homoserine derivatives followed by mild acidic as well as mild alkaline hydrolysis. The reduction of keto group of kynurenine to hydroxy one was achieved by controlled potential electrolysis at —1.05 Volts. In order to understand the mechanism of hydrolysis some model com­ pounds related to kynurenine peptides were also synthesized and studied. Hydrolysis of y-(o-aminophenyl)-homoserine peptides in acidic media is related only to the assistance of y-hydroxy function, whereas in alkaline media also aromatic amino group is involved.