Potential inhibitors of metalloproteinases (MMPs) and phospholipases from Nemopilema nomurai jellyfish peptides: An in-silico pharmacokinetics and molecular docking studies

Jellyfish stings, especially from Nemopilema nomurai, pose serious health risks due to its venom toxins like metalloproteinases (MMPs) and phospholipases A2 (PLAs A2). Thes toxin can induce severe reactions such as pain, tissue necrosis, inflammation, and in extreme cases, cardiac arrest. While the exact mechanisms of toxicity are not fully understood, MMPs and PLA2 enzymes are known to contribute significantly to tissue damage and inflammation. Thus, the inhibition of these toxins could reduce venom toxicity and provide new treatment options for jellyfish envenomation. This study utilized pharma informatic to evaluate Nemopilema nomurai jellyfish-derived peptides against Nemopilema nomurai venom toxins (metalloproteinase and phospholipase). After profiling absorption, distribution, metabolism, excretion, and toxicity (ADMET) parameters, two peptides, DN26779_N and DN26779_Q, were selected for docking analysis. DN26779_N exhibited higher binding energy to metalloproteinase (−13.3), and phospholipase (−12.6) than DN26779_Q. Molecular dynamics simulations confirmed the stability of these interactions, driven by hydrophobic affinity and hydrogen bonding. Overall, DN26779_N and DN26779_Q demonstrate significant potential as inhibitors of metalloproteinase, and phospholipase A2, presenting promising therapeutic avenues for treating and addressing jellyfish envenomation.