Synthesis of lipidic amino acid and dipeptide inhibitors of human platelet phospholipase A2

Abstract
Phospholipases A2 (PLA2s) catalyze the hydrolysis of glycerophospholipids at the sn-2 position, and their inhibition is considered a rational approach for the prevention and treatment of inflammation. A number of amides and esters of alpha-amino acids with saturated linear side chains, esters of alpha-amino alcohols and derivatives of lipidic peptides were prepared and tested against secreted humal platelet phospholipase A2. Among the compounds tested the amides of free amino acids with long-chain amines presented the highest in vitro inhibitory activity.