Study of Antiproteinase Activity of Acylated Derivatives of Bowman-Birk Soybean Proteinase Inhibitor

E. V. Malykh and N. I. Larionova^*

Department of Chemical Enzymology, School of Chemistry, Lomonosov Moscow State University, Moscow, 119992 Russia; fax: (095) 939-5417; E-mail: nilar@enzyme.chem.msu.ru

^* To whom correspondence should be addressed.

Received June 20, 2001; Revision received July 16, 2001

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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.

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KEY WORDS: Bowman-Birk inhibitor, acylation, unsaturated fatty acids, inhibition constant, trypsin, alpha-chymotrypsin, human leukocyte elastase

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