Synthesis and PLA2-inhibitory properties of 2(R)-acetamido-alkylphosphomethanols with a variable aggregate anchor

Acylamino inhibitors of 14 kDa-PLA2 were synthesized which differ in the moiety that is not bound into the enzymeʹs active site but immersed in the lipid aggregate when a ternary inhibitory complex is formed. Our results indicate that this part of the inhibitors does not significantly influence inhibitory properties as long the amphiphilic character is retained. So, inhibitory and biophysical properties should be variable independently.