phospholipase a2

Phospholipase A2 (PLA2) is an enzyme that hydrolyzes fatty acids present in the sn-2 position of phospholipids, and is closely related to lipid metabolism and immune function.

Melittin free acid, a basic 26-amino-acid polypeptide, constitutes the primary active component of honeybee venom and serves as a phospholipase A2 (PLA2) activator. Exhibiting a broad-spectrum antifungal effect, it presents MIC values ranging from 0.4-60 μM. Its mechanism includes inducing cell apoptosis, inhibiting (1,3)-β-D-glucan synthase, and engaging in multiple pathways [1] [2].

The sPLA2-IIA Inhibitor is a cyclic pentapeptide analog of FLSYK, specifically cyclic 2-Nal-Leu-Ser-2-Nal-Arg (c2), which interacts with human IIA phospholipase A2 (hGIIA) to impede its ester bond hydrolyzing function. As part of the esterase superfamily, sPLA2 enzymatically cleaves the sn-2 ester bond in glycerophospholipids, releasing arachidonic acid and lysophospholipids[1].

Anti-Inflammatory Peptide 1 Acetate (C45H82N12O14S2) possesses a potent anti-inflammatory activity in vivo and is a strong inhibitor of phospholipase A2 (PLA2), whose increased presence and activity results in inflammation and pain at certain bodily sites

Antiflammin P2 is a nonapeptide fragment of lipocortin I which has no phospholipase A2 inhibitory and anti-inflammatory activity.