Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Chymotrypsin / antagonists & inhibitors*
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Lignans / pharmacology*
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Plants, Medicinal / chemistry
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Prolyl Oligopeptidases
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Serine Endopeptidases / drug effects
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Serine Proteinase Inhibitors / pharmacology
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Thrombin / drug effects
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Vitex / chemistry*
Substances
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Lignans
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Serine Proteinase Inhibitors
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Serine Endopeptidases
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Chymotrypsin
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alpha-chymotrypsin
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Prolyl Oligopeptidases
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Thrombin