A comprehensive study on the mechanism of inhibition of serine proteases by benzamidines based on quantitative structure-activity relationship studies.
Based on quantitative structure-activity relationship studies, investigation is made on the mechanism of inhibition of serine proteases, i.e., thrombin, plasmin, trypsin, and complement, by benzamidines. It is found that inhibitions of all the four enzymes, thrombin, plasmin, trypsin and complement, involve hydrophobic interaction in general but they do not involve electronic interaction in all the cases. In the cases where the electronic interaction is involved the mode of interaction is not necessarily the same. The electronic interaction depends upon the kind and the source of the enzyme.
D000578:Amidines / Q000494:pharmacology*; D000818:Animals; D001550:Benzamidines / Q000494:pharmacology*; D002417:Cattle; D003169:Complement Inactivator Proteins; D010450:Endopeptidases; D005341:Fibrinolysin / Q000037:antagonists & inhibitors; D006168:Guinea Pigs; D006801:Humans; D011480:Protease Inhibitors; D012697:Serine Endopeptidases; D013329:Structure-Activity Relationship; D013917:Thrombin / Q000037:antagonists & inhibitors; D014361:Trypsin Inhibitors
D000578:Amidines; D001550:Benzamidines; D003169:Complement Inactivator Proteins; D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; D010450:Endopeptidases; D012697:Serine Endopeptidases; D013917:Thrombin; D005341:Fibrinolysin