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.
Malykh
E V
EV
Department of Chemical Enzymology, School of Chemistry, Lomonosov Moscow State University, Moscow, 119992 Russia.
Larionova
N I
NI
D000215:Acylation; D002918:Chymotrypsin / Q000494:pharmacology; D002942:Circular Dichroism; D005227:Fatty Acids / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D019272:Leukocyte Elastase / Q000378:metabolism; D008958:Models, Molecular; D011480:Protease Inhibitors / Q000494:pharmacology*; D017434:Protein Structure, Tertiary; D014357:Trypsin / Q000494:pharmacology; D014358:Trypsin Inhibitor, Bowman-Birk Soybean / Q000737:chemistry* / Q000494:pharmacology*
D005227:Fatty Acids; D011480:Protease Inhibitors; D014358:Trypsin Inhibitor, Bowman-Birk Soybean; D002918:Chymotrypsin; C117608:alpha-chymotrypsin; D019272:Leukocyte Elastase; D014357:Trypsin