Study of antiproteinase activity of acylated derivatives of Bowman-Birk soybean proteinase inhibitor

The effect of acylation of Bowman-Birk soybean proteinase inhibitor (BBI) by derivatives of various unsaturated fatty acids on inhibition of trypsin, alpha-chymotrypsin, and human leukocyte elastase was investigated. Inhibition (K-i) and kinetic (k(ass), k(diss)) constants of interaction between proteases and acylated BBI derivatives were determined. For mono-, di-, and triacylated BBI derivatives, insertion of two oleic residues into the BBI molecule was demonstrated to be more potent for exhibiting antiproteinase activity.