Thioetheramide-PC is a structurally modified phospholipid that functions as a competitive, reversible inhibitor of secretory phospholipase A2 (sPLA2). The IC50 value for thioetheramide-PC is 2 μM at a substrate concentration of 0.5 mM. In addition to binding to the catalytic site of sPLA2, thioetheramide-PC also binds to the activator site of this enzyme. The binding of thioetheramide-PC to the activator site is tighter than its binding to the catalytic site. The result of this dual interaction is that at low concentrations thioetheramide-PC may activate phospholipase activity rather than inhibiting it.
[1] yu l, deems r a, hajdu j, et al. the interaction of phospholipase a2 with phospholipid analogues and inhibitors[j]. journal of biological chemistry, 1990, 265(5): 2657-2664.
[2] balsinde j, balboa m a, insel p a, et al. regulation and inhibition of phospholipase a2[j]. annual review of pharmacology and toxicology, 1999, 39(1): 175-189.
[3] mallat z, lambeau g, tedgui a. lipoprotein-associated and secreted phospholipases a2 in cardiovascular disease[j]. circulation, 2010, 122(21): 2183-2200.
