Abstract
Quantitative structure-activity relationship (QSAR) study of human factor Xa inhibitor N 2 -aroylanthranilamides, recently reported by Yee et al. ( J. Med. Chem. , 43 , 873-882), has been performed using principal component factor analysis as the preprocessing step. The study reveals that presence of electron-donating R2 substituent at the para position (with respect to the amide linkage) is conducive to the binding affinity, whereas a meta R2 substituent decreases the affinity. Again, electron-donating R1 substituents with less bulk and optimum hydrophilic-lipophilic balance (particularly, methyl and methoxy groups) favor the activity. The study further suggests that electron-withdrawing R3 substituents are detrimental for the activity, whereas bulkier R4 substituents (particularly NHSO 2 Me group) increase the activity.