ArticleArchives of toxicology2026
Targeting marine jellyfish toxins: development of metalloproteinase inhibitors through a specific method for protease substrate identification.
Article in Archives of toxicology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The venom of hazardous jellyfish contains harmful substances to human health, such as metalloproteinases, which are challenging to purify. Therefore, identifying substrate sequences using crude venom is crucial for the development of peptide inhibitors. This study utilized a designed peptide library and an abundance-based hydrolysis product analysis approach to identify the substrate sequences of toxin metalloproteinases from Nemopilema nomurai nematocyst venom (NnNV) and further modified these sequences into peptide inhibitors. Specifically, a peptide library comprising 41 potential substrate sequences was constructed and incubated with NnNV. 12 substrate sequences and 14 cleavage sites were identified from the hydrolysis products. In the design of peptide inhibitors, thiol (-SH) and phosphate groups (-PO
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