QSAR of human factor Xa inhibitor N2-aroylanthranilamides using principal component factor analysis.
Quantitative structure-activity relationship (QSAR) study of human factor Xa inhibitor N2-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 NHSO2Me group) increase the activity.
Roy
Kunal
K
Department of Pharmaceutical Technology, Jadavpur University, Calcutta, India. kunalroy_in@yahoo.com
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A U
AU
Sengupta
Chandana
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D000990:Antithrombin III / Q000737:chemistry* / Q000493:pharmacokinetics; D006801:Humans; D025341:Principal Component Analysis / Q000379:methods*; D021281:Quantitative Structure-Activity Relationship; D062367:ortho-Aminobenzoates / Q000737:chemistry* / Q000493:pharmacokinetics
D062367:ortho-Aminobenzoates; D000990:Antithrombin III; C000219:anthranilamide