alpha-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 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.
Arif Lodhi
Muhammad
M
Dr. Panjwani Center for Molecular Medicine and Drug Research, University of Karachi, Karachi-75270, Pakistan.
Iqbal Choudhary
M
M
Malik
Abdul
A
Ahmad
Saeed
S
D002918:Chymotrypsin / Q000037:antagonists & inhibitors*; D017705:Lignans / Q000494:pharmacology*; D010946:Plants, Medicinal / Q000737:chemistry; D000085822:Prolyl Oligopeptidases; D012697:Serine Endopeptidases / Q000187:drug effects; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology; D013917:Thrombin / Q000187:drug effects; D020950:Vitex / Q000737:chemistry*
D017705:Lignans; D015842:Serine Proteinase Inhibitors; D012697:Serine Endopeptidases; D002918:Chymotrypsin; C117608:alpha-chymotrypsin; D000085822:Prolyl Oligopeptidases; D013917:Thrombin