Characterization of Novel ACE-Inhibitory Peptides from <i>Nemopilema nomurai</i> Jellyfish Venom Hydrolysate: In Vitro and In Silico Approaches.

ABSTRACT: The venom of Nemopilema nomurai jellyfish represents a promising source of bioactive compounds with potential pharmacological applications. In our previous work, we identified two novel angiotensin-converting enzyme (ACE)-inhibitory peptides-IVGRPLANG (896.48 Da) and IGDEPRHQYL (1227.65 Da)-isolated from N. nomurai venom hydrolysates via papain digestion. In this study, we conducted a detailed biochemical and computational characterization of these peptides. The IC₅₀ values were determined to be 23.81 µM for IVGRPLANG and 5.68 µM for IGDEPRHQYL. Kinetic analysis using Lineweaver-Burk plots revealed that both peptides act as competitive ACE inhibitors, with calculated inhibition constants (K_i) of 51.38 µM and 5.45 µM, respectively. To assess the structura

SUBMITTER: Prakash RLM 

PROVIDER: S-EPMC12298423 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature