The inhibitory mechanism of bovine pancreatic phospholipase A2 by aldehyde terpenoids

Article abstract of DOI:10.1016/S0040-4020(98)01197-1

We established the stereoselective synthesis of (E)-3-methoxycarbonyl- 2,4,6-trienal compound A and discovered that the compound A showed more powerful inhibitory activity toward phospholipase A₂(PLA₂) from bovine pancreas than manoalide which is a typical PLA₂ inhibitor. As the inhibitory mechanism of PLA₂ by A, the irreversible formation of dihydropyridine derivative resulting from the reaction of A with lysine residues in PLA₂ was proposed based on the model reactions. Furthermore, A was found to selectively modify Lys56 which is included in the interfacial recognition site of this enzyme by the MALDI-TOF-MS peptide mapping analyses.