The Metalloproteases Meprin a and b: Pathophysiological Roles in Inflammation, Cardiovascular Disease, Cancer, and Fibrosis - Proteinases as Drug Targets - page 56

K i 2.0 × 10 -8 M
2.3 × 10 -9 M

K i 2.0 × 10 -6 M
2.3 × 10 -7 M

K i 4.4 × 10 -6 M
4.6 × 10 -7 M

K i 1.8 × 10 -5 M
2.2 × 10 -6 M

K i 1.4 × 10 -7 M
9.9 × 10 -9 M

K i 8.9 × 10 -6 M
7.1 × 10 -7 M

K i 4.0 × 10 -7 M
3.7 × 10 -8 M

K i 7.4 × 10 -6 M
7.6 × 10 -7 M

K i 5.3 × 10 -7 M
5.1 × 10 -8 M

K i 1.4 × 10 -5 M
1.2 × 10 -6 M

n. i. n. i.

K i 1.6 × 10 -6 M
2.6 × 10 -8 M

IC 50 1.6 × 10 -3 M
1.2 × 10 -4 M

K i 2.2 × 10 -6 M
3.5 × 10 -8 M

IC 50 4 × 10 -4 M
1 × 10 -4 M

K i 1.5 × 10 -6 M
2.7 × 10 -7 M

IC 50 2 × 10 -4 M
1 × 10 -4 M

K i 7.4 × 10 -4 M
6.0 × 10 -6 M

K i 4.1 × 10 -4 M
1.2 × 10 -5 M

Figure 2.7 Small non-peptidic inhibitors of human meprins. Displayed are the projec-

tion formulae and inhibition constants of meprin inhibitors. 54 The K i and
IC 50 were calculated using GraFit 4.0 (Erithacus Software). In general,
meprin a revealed a higher sensitivity towards these compounds compared to
meprin b. Themost effective inhibitor is the naturally occurring hydroxamate
actinonin. n.i., no inhibition; PLG-NHOH, Pro-Leu-Glyhydroxamate.