Inactivation of trypsin-like proteases by sulfonylation. Variation of positively charged group and inhibitor length.
Attempts to achieve selective inactivation of serine proteases of closely related specificity (trypsin-like) by aryl sulfonylation have been extended. Nitrophenyl esters of benzenesulfonic acid and phenylmethanesulfonic acid containing various positively charged groups have been synthesized and examined as inactivators of trypsin, thrombin, plasmin, plasma kallikrein, and urokinase. Examples of selective inactivation by isothiouronium derivatives were found and attributed to differences among these enzymes in geometry and flexibility of the primary specificity sites.
D055598:Chemical Phenomena; D002621:Chemistry; D009596:Nitrophenols / Q000138:chemical synthesis; D011480:Protease Inhibitors; D013329:Structure-Activity Relationship; D013451:Sulfonic Acids / Q000138:chemical synthesis; D013997:Time Factors
D009596:Nitrophenols; D011480:Protease Inhibitors; D013451:Sulfonic Acids