Chemical substitutions of the reactive site leucine residue in soybean Bowman-Birk proteinase inhibitor with other amino acids.

摘要: A method of exchanging amino acid residue (P1 residue) which determines primarily the inhibitory specificity a proteinase inhibitor is described. Leu43 at chymotrypsin reactive site Bowman-Birk soybean was removed by limited proteolysis Leu43-Ser44 bond followed carboxypeptidase digestion. An appropriate methyl ester introduced into this position water-soluble carbodiimide. Derivatives having esters Gly, Ala, Val, Met, Leu, Phe, Trp, or D-Trp 43 were prepared and shown to restore activity various extents. This provides new approach study structure-function relationship inhibitors prepare novel inhibitors.