α-Chymotrypsin inhibition studies on the lignans from Vitex negundo Linn

The lignans (1-8) isolated from the roots of Vitex negundo Linn. were screened against the serine proteases α-chymotrypsin, thrombin and prolyl endopeptidase. Compounds 3 and 4 were found to be active only against α-chymotrypsin and were noncompetitive and competitive inhibitors of the enzyme, respe...

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Published inJournal of enzyme inhibition and medicinal chemistry Vol. 23; no. 3; pp. 400 - 405
Main Authors Arif Lodhi, Muhammad, Azhar-ul-Haq, Iqbal Choudhary, M., Malik, Abdul, Ahmad, Saeed
Format Journal Article
LanguageEnglish
Published England Informa UK Ltd 01.06.2008
Subjects
Chymotrypsin - antagonists & inhibitors
Lignans - pharmacology
Plants, Medicinal - chemistry
Serine Endopeptidases - drug effects
Serine Proteinase Inhibitors - pharmacology
Thrombin - drug effects
Vitex - chemistry
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Summary:The lignans (1-8) isolated from the roots of Vitex negundo Linn. were screened against the serine proteases α-chymotrypsin, thrombin and prolyl endopeptidase. Compounds 3 and 4 were found to be active only against α-chymotrypsin and were noncompetitive and competitive inhibitors of the enzyme, respectively. Ki values were found to be in the range 31.75-47.11 μM.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1475-6366
1475-6374
DOI:10.1080/14756360701584653