[Hydrophobic interactions of serine proteases with low molecular compounds: role of the S'2-site in substrate activation and interaction with serpines].

An attempt is made to simulate the P1-P'2 site of the reactive centre of protein inhibitors of serine proteases (serpines). On the basis of data from literature structure requirements are formulated and compound 1,5 bis-dibenzyl-aminopentane is synthesized. It may simultaneously interact with S1- and S'2-sites of chymotrypsin and contains no bonds adequate to the hydrolytic centre of proteinase. The compound is studied for its effect on hydrolysis of low-molecular substrates and proteins by chymotrypsin. Results obtained are discussed as well as the possible role of the S'2-binding site in the substrate activation of serine proteinases and their interaction with serpines.