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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Veröffentlicht in:	Journal of enzyme inhibition and medicinal chemistry 2008-06, Vol.23 (3), p.400-405
Hauptverfasser:	Arif Lodhi, Muhammad, Azhar-ul-Haq, Iqbal Choudhary, M., Malik, Abdul, Ahmad, Saeed
Format:	Artikel
Sprache:	eng
Schlagworte:	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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Beschreibung
Zusammenfassung:	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.
ISSN:	1475-6366 1475-6374
DOI:	10.1080/14756360701584653