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• W2000975579 abstract "Abstract Secretory phospholipases A 2 (sPLA 2 s) are implicated in the pathogenesis of several inflammation diseases, such as rheumatoid arthritis, septic shock, psoriasis, and asthma. Thus, an understanding of their inactivation mechanisms could be useful for the development of new classes of chemical selective inhibitors. In the marine environment, several bioactive terpenoids possess interesting anti‐inflammatory activity, often through covalent and/or noncovalent inactivation of sPLA 2 . Herein, we report the molecular mechanism of human group IIA phospholipase A 2 (sPLA 2 ‐IIA) inactivation by Scalaradial (SLD), a marine 1,4‐dialdehyde terpenoid isolated from the sponge Cacospongia mollior and endowed with a significant anti‐inflammatory profile. Our results have been collected by a combination of biochemical approaches, advanced mass spectrometry, surface plasmon resonance, and molecular modeling. These suggest that SLD acts as a competitive inhibitor. Indeed, the sPLA 2 ‐IIA inactivation process seems to be driven by the noncovalent recognition process of SLD in the enzyme active site and by chelation of the catalytic calcium ion. In contrast, covalent modification of the enzyme by the SLD dialdehyde moiety emerges as only a minor side event in the ligand–enzyme interaction. These results could be helpful for the rational design of new PLA 2 inhibitors that would be able to selectively target the enzyme active site." @default.
• W2000975579 created "2016-06-24" @default.
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• W2000975579 date "2012-09-24" @default.
• W2000975579 modified "2023-10-10" @default.
• W2000975579 title "The Inactivation Mechanism of Human Group IIA Phospholipase A₂by Scalaradial" @default.
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• W2000975579 doi "https://doi.org/10.1002/cbic.201200453" @default.
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