Journal of Enzyme Inhibition and Medicinal Chemistry 2008-Jun
alpha-Chymotrypsin inhibition studies on the lignans from Vitex negundo Linn.
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The lignans (1-8) isolated from the roots of Vitex negundo Linn. were screened against the serine proteases alpha-chymotrypsin, thrombin and prolyl endopeptidase. Compounds 3 and 4 were found to be active only against alpha-chymotrypsin and were noncompetitive and competitive inhibitors of the enzyme, respectively. Ki values were found to be in the range 31.75-47.11 microM.
