| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1355854 | Bioorganic Chemistry | 2009 | 5 Pages |
Petrosaspongiolides are sponge metabolites belonging to the family of the γ-hydroxybutenolide marine terpenoids. They possess a remarkable in vitro and in vivo anti-inflammatory profile, due to the specific inhibition of group II and III secretory phospholipase A2 enzymes, and for this reason can be considered as potential lead for the development of anti-inflammatory drugs. The molecular mechanism of bee venom phospholipase A2 inactivation has been identified, and the ligand–enzyme complex formation is guided by either non-covalent and covalent interactions. In this work we have analyzed the conformational changes induced by petrosaspongiolide R on the bee venom phospholipase A2 topology during the molecular recognition process, through the application of limited proteolysis and mass spectrometric methodologies. The results are indicative of structural changes at the N- and C-terminal domains producing a more compact conformational arrangement of the enzyme.
Graphical abstractPetrosaspongiolide R, a marine natural inhibitor of bee venom PLA2, induces conformational changes on the N- and C-terminal regions of its target enzyme.Figure optionsDownload full-size imageDownload as PowerPoint slide
