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. 2021 Jan 21;11:614928. doi: 10.3389/fphar.2020.614928

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Copyright © 2021 Simon, Wang, Avsec, Obreza, Yousefi and Mlinaric-Rascan.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Comparative activity of compounds against five different serine proteases. Compound 1, 3, TPCK, and TLCK were incubated with trypsin (Try), α-chymotrypsin (α-Chy), human neutrophil elastase (HNE), cathepsin G (CatG), and proteinase 3 (PR3) at 37 °C for 30 min. Subsequently, reactions were started by adding an enzyme-specific substrate. Substrate hydrolysis was monitored in a kinetic mode for 60 min. The initial rates of reactions were used to calculate the % relative inhibition of the enzymes. Results are presented as mean ± SEM of 3 independent experiments, run in duplicate. (A) Relative inhibition (%) of serine proteases for 10 µM compound 1, 3, TPCK, and TLCK. (B) Relative inhibition (%) of serine proteases for 25 µM compound 1, 3, TPCK, and TLCK. (C) Relative inhibition (%) of serine proteases for 50 µM compound 1, 3, TPCK, and TLCK.