{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T20:00:58Z","timestamp":1790280058939,"version":"4.1.0"},"reference-count":59,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2024,9,20]],"date-time":"2024-09-20T00:00:00Z","timestamp":1726790400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Ministry of Education","award":["RS-2023-00276023"],"award-info":[{"award-number":["RS-2023-00276023"]}]},{"name":"Ministry of Education","award":["NRF-2021R1I1A306005711"],"award-info":[{"award-number":["NRF-2021R1I1A306005711"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>Recently, jellyfish venom has gained attention as a promising reservoir of pharmacologically active compounds, with potential applications in new drug development. In this investigation, novel peptides, isolated from the hydrolysates of Nemopilema nomurai jellyfish venom (NnV), demonstrate potent inhibitory activities against angiotensin-converting enzyme (ACE). Proteolytic enzymes\u2014specifically, papain and protamex\u2014were utilized for the hydrolysis under optimized enzymatic conditions, determined by assessing the degree of hydrolysis through the ninhydrin test. Comparative analyses revealed that papain treatment exhibited a notably higher degree of NnV hydrolysis compared to protamex treatment. ACE inhibitory activity was quantified using ACE kit-WST, indicating a substantial inhibitory effect of 76.31% for the papain-digested NnV crude hydrolysate, which was validated by captopril as a positive control. The separation of the NnV-hydrolysate using DEAE sepharose weak-anion-exchange chromatography revealed nine peaks under a 0\u20131 M NaCl stepwise gradient, with peak no. 3 displaying the highest ACE inhibition of 96%. The further purification of peak no. 3 through ODS-C18 column reverse-phase high-performance liquid chromatography resulted in five sub-peaks (3.1, 3.2, 3.3, 3.4, and 3.5), among which 3.2 exhibited the most significant inhibitory activity of 95.74%. The subsequent analysis of the active peak (3.2) using MALDI\u2013TOF\/MS identified two peptides with distinct molecular weights of 896.48 and 1227.651. The peptide sequence determined by MS\/MS analysis revealed them as IVGRPLANG and IGDEPRHQYL. The docking studies of the two ACE-inhibitory peptides for ACE molecule demonstrated a binding affinity of \u221251.4 \u00b1 2.5 and \u221262.3 \u00b1 3.3 using the HADDOCK scoring function.<\/jats:p>","DOI":"10.3390\/toxins16090410","type":"journal-article","created":{"date-parts":[[2024,9,20]],"date-time":"2024-09-20T10:49:48Z","timestamp":1726829388000},"page":"410","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Identification of New Angiotensin-Converting Enzyme Inhibitory Peptides Isolated from the Hydrolysate of the Venom of Nemopilema nomurai Jellyfish"],"prefix":"10.3390","volume":"16","author":[{"given":"Ramachandran Loganathan","family":"Mohan Prakash","sequence":"first","affiliation":[{"name":"College of Veterinary Medicine, Gyeongsang National University, Jinju 52828, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Deva Asirvatham","family":"Ravi","sequence":"additional","affiliation":[{"name":"College of Veterinary Medicine, Gyeongsang National University, Jinju 52828, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7228-3340","authenticated-orcid":false,"given":"Du Hyeon","family":"Hwang","sequence":"additional","affiliation":[{"name":"College of Veterinary Medicine, Gyeongsang National University, Jinju 52828, Republic of Korea"},{"name":"Institute of Animal Medicine, Gyeongsang National University, Jinju 52828, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5114-5096","authenticated-orcid":false,"given":"Changkeun","family":"Kang","sequence":"additional","affiliation":[{"name":"College of Veterinary Medicine, Gyeongsang National University, Jinju 52828, Republic of Korea"},{"name":"Institute of Animal Medicine, Gyeongsang National University, Jinju 52828, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3356-3072","authenticated-orcid":false,"given":"Euikyung","family":"Kim","sequence":"additional","affiliation":[{"name":"College of Veterinary Medicine, Gyeongsang National University, Jinju 52828, Republic of Korea"},{"name":"Institute of Animal Medicine, Gyeongsang National University, Jinju 52828, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,9,20]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"c125","DOI":"10.1159\/000232592","article-title":"Drug development: From concept to marketing!","volume":"113","author":"Tamimi","year":"2009","journal-title":"Nephron Clin. Pract."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1146\/annurev.pa.08.040168.001503","article-title":"Pharmacology of peptides and proteins in snake venoms","volume":"8","year":"1968","journal-title":"Annu. Rev. Pharmacol."},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Bordon, K.D.C.F., Cologna, C.T., Fornari-Baldo, E.C., Pinheiro-J\u00fanior, E.L., Cerni, F.A., Amorim, F.G., Anjolette, F.A.P., Cordeiro, F.A., Wiezel, G.A., and Cardoso, I.A. (2020). From animal poisons and venoms to medicines: Achievements, challenges and perspectives in drug discovery. Front. Pharmacol., 11.","DOI":"10.3389\/fphar.2020.01132"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1161\/HYPERTENSIONAHA.119.14240","article-title":"High blood pressure and cardiovascular disease","volume":"75","author":"Fuchs","year":"2020","journal-title":"Hypertension"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1038\/s41569-023-00964-1","article-title":"Maffia Immune and inflammatory mechanisms in hypertension","volume":"21","author":"Guzik","year":"2024","journal-title":"Nat. Rev. Cardiol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"245","DOI":"10.7326\/M14-1753","article-title":"Cardiovascular mortality associated with 5 leading risk factors: National and state preventable fractions estimated from survey data","volume":"163","author":"Patel","year":"2015","journal-title":"Ann. Intern. Med."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1016\/S0140-6736(14)60616-4","article-title":"Contribution of Six Risk Factors to Achieving the 25 \u00d7 25 Non-Communicable Disease Mortality Reduction Target: A Modelling Study","volume":"384","author":"Kontis","year":"2014","journal-title":"Lancet"},{"key":"ref_8","unstructured":"World Health Organization (2013). NCD Global Monitoring Framework, WHO."},{"key":"ref_9","first-page":"18014","article-title":"Hypertension","volume":"4","author":"Oparil","year":"2018","journal-title":"Nat. Rev."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"3021","DOI":"10.1093\/eurheartj\/ehy339","article-title":"2018 ESC\/ESH Guidelines for the management of arterial hypertension: The Task Force for the management of arterial hypertension of the European Society of Cardiology (ESC) and the European Society of Hypertension (ESH)","volume":"39","author":"Williams","year":"2018","journal-title":"Eur. Heart J."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1913","DOI":"10.1139\/z88-280","article-title":"Interactions of fish and pelagic coelenterates","volume":"66","author":"Arai","year":"1988","journal-title":"Can. J. Zool."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1016\/0041-0101(77)90016-2","article-title":"Investigations into the cardiotoxicity of a toxin from the nematocysts of the jellyfish, Cyanea capillata","volume":"15","author":"Walker","year":"1977","journal-title":"Toxicon"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/j.toxicon.2016.04.050","article-title":"In vitro angiotensin I converting enzyme inhibition by a peptide isolated from Chiropsalmus quadrigatus Haeckel (box jellyfish) venom hydrolysate","volume":"119","author":"So","year":"2016","journal-title":"Toxicon"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1016\/j.carbpol.2016.12.031","article-title":"Structural characterization and immunomodulatory activity of a new polysaccharide from jellyfish","volume":"159","author":"Li","year":"2017","journal-title":"Carbohydr. Polym."},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Suganthi, K., and Bragadeeswaran, S. (2012). Antimicrobial and immunomodulatory activities of jellyfish (Chrysaora quinquecirrha) venom. Prospects in Bioscience: Addressing the Issues, Springer.","DOI":"10.1007\/978-81-322-0810-5_34"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1986","DOI":"10.1016\/j.biopha.2016.11.010","article-title":"Evaluation of anti-proliferative and anti-inflammatory activities of Pelagia noctiluca venom in Lipopolysaccharide\/Interferon-\u03b3 stimulated RAW264.7 macrophages","volume":"84","author":"Ayed","year":"2016","journal-title":"Biomed. Pharmaco."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1080\/13880200601026325","article-title":"Antimicrobial, antiprotozoal, and toxic activities of cnidarian extracts from the Mexican Caribbean Sea","volume":"45","year":"2007","journal-title":"Pharm. Bio."},{"key":"ref_18","first-page":"36","article-title":"Taxonomic Review of Three Japanese Species of Edible Jellyfish (Scyphozoa: Rhizostomeae)","volume":"51","author":"Omori","year":"2004","journal-title":"Plankt. Biol. Ecol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"161","DOI":"10.3354\/meps307161","article-title":"Unusual Population Explosion of the Giant Jellyfish Nemopilema Nomurai (Scyphozoa: Rhizostomeae) in East Asian Waters","volume":"307","author":"Kawahara","year":"2006","journal-title":"Mar. Ecol. Prog. Ser."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1127","DOI":"10.1080\/21691401.2018.1480490","article-title":"Upcycling of jellyfish (Nemopilema nomurai) sea wastes as highly valuable reducing agents for green synthesis of gold nanoparticles and their antitumor and anti-inflammatory activity","volume":"46","author":"Ahn","year":"2018","journal-title":"Artif. Cells Nanomed. Biotechnol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"2752716","DOI":"10.1155\/2017\/2752716","article-title":"Anticancer effect of Nemopilema nomurai jellyfish venom on HepG2 cells and a tumor xenograft animal model","volume":"2017","author":"Lee","year":"2017","journal-title":"Evid. Based Complement. Altern. Med."},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Choudhary, I., Lee, H., Pyo, M.J., Heo, Y., Chae, J., Yum, S.S., Kang, C., and Kim, E. (2018). Proteomic investigation to identify anticancer targets of Nemopilema nomurai jellyfish venom in human hepatocarcinoma HepG2 cells. Toxins, 10.","DOI":"10.3390\/toxins10050194"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"2808","DOI":"10.1038\/s41598-018-20724-3","article-title":"Nemopilema nomurai jellyfish venom exerts an anti-metastatic effect by inhibiting smad-and NF-\u03baB-Mediated epithelial\u2013mesenchymal transition in HepG2 cells","volume":"8","author":"Lee","year":"2018","journal-title":"Sci. Rep"},{"key":"ref_24","first-page":"174","article-title":"ACE-inhibitory properties of proteolytic hydrolysates from giant jellyfish Nemopilema nomurai","volume":"14","author":"Yoon","year":"2011","journal-title":"Fish. Aquat. Sci."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/j.cbpc.2009.03.003","article-title":"Cytotoxicity and hemolytic activity of jellyfish Nemopilema nomurai (Scyphozoa: Rhizostomeae) venom","volume":"150","author":"Kang","year":"2009","journal-title":"Comp. Biochem. Physiol. Part C Toxicol. Pharmacol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/j.toxlet.2004.09.004","article-title":"The in vivo cardiovascular effects of the Irukandji jellyfish (Carukia barnesi) nematocyst venom and a tentacle extract in rats","volume":"155","author":"Ramasamy","year":"2005","journal-title":"Toxicol. Lett."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1016\/S0041-0101(03)00010-2","article-title":"Haemodynamic effects of the crude venom from nematocysts of the box-jellyfish Chiropsalmus quadrigatus (Habu-kurage) in anaesthetized rabbits","volume":"41","author":"Koyama","year":"2003","journal-title":"Toxicon"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1177\/0310057X0203000504","article-title":"Effects of diltiazem on in vitro cardiovascular actions of crude venom obtained from okinawan box-jellyfish (habu-kurage), Chiropsalmus quadrigatus","volume":"30","author":"Sakanashi","year":"2002","journal-title":"Anaesth. Intensiv. Care"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1126\/science.191908","article-title":"Design of specific inhibitors of angiotensin-converting enzyme: New class of orally active antihypertensive agents","volume":"196","author":"Ondetti","year":"1977","journal-title":"Science"},{"key":"ref_30","first-page":"525","article-title":"Characteristics and Use of Protein Hydrolysates (Review)","volume":"36","author":"Nekliudov","year":"2000","journal-title":"Prikl. Biokhimiia Mikrobiol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/bs.afnr.2016.10.003","article-title":"Protein hydrolysates and biopeptides: Production, biological activities, and applications in foods and health benefits. A review","volume":"81","author":"Nasri","year":"2017","journal-title":"Adv. Food Nutr. Res."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/S1385-8947(00)00197-2","article-title":"A modified Langmuir model for the prediction of the effects of ionic strength on the equilibrium characteristics of protein adsorption onto ion exchange\/affinity adsorbents","volume":"81","author":"Lan","year":"2001","journal-title":"Chem. Eng. J."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1007\/s00449-007-0185-1","article-title":"Separation of phycocyanin from Spirulina platensis using ion exchange chromatography","volume":"31","author":"Silveira","year":"2008","journal-title":"Bioprocess Biosyst. Eng."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/j.procbio.2017.04.032","article-title":"In silico analysis and antihypertensive effect of ACE-inhibitory peptides from smooth-hound viscera protein hydrolysate: Enzyme-peptide interaction study using molecular docking simulation","volume":"58","author":"Abdelhedi","year":"2017","journal-title":"Process Biochem."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"765","DOI":"10.3390\/nu3090765","article-title":"Bioactive peptides from muscle sources: Meat and fish","volume":"3","author":"Ryan","year":"2011","journal-title":"Nutrients"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1016\/j.atherosclerosis.2008.06.019","article-title":"Nutritional and nutraceutical approaches to dyslipidemia and atherosclerosis prevention: Focus on dietary proteins","volume":"203","author":"Sirtori","year":"2009","journal-title":"Atherosclerosis"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1007\/s00217-017-2968-1","article-title":"Affinity purification of angiotensin-converting enzyme inhibitory peptides from Volutharpa ampullacea perryi protein hydrolysate using Zn-SBA-15 immobilized ACE","volume":"244","author":"Sun","year":"2017","journal-title":"Eur. Food Res. Technol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"e13123","DOI":"10.1111\/jfpp.13123","article-title":"Isolation and purification of antioxidant and ACE-inhibitory peptides from Yak (Bos grunniens) skin","volume":"41","author":"Tian","year":"2017","journal-title":"J. Food Process. Preserv."},{"key":"ref_39","doi-asserted-by":"crossref","unstructured":"Mane, S., and Jamdar, S. (2017). Purification and identification of Ace-inhibitory peptides from poultry viscera protein hydrolysate. J. Food Biochem., 41.","DOI":"10.1111\/jfbc.12275"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1016\/j.tifs.2019.04.002","article-title":"Basic and recent advances in marine antihypertensive peptides: Production, structure-activity relationship and bioavailability","volume":"88","author":"Abdelhedi","year":"2019","journal-title":"Trends Food Sci. Technol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.foodchem.2011.07.011","article-title":"Studies on purification and the molecular mechanism of a novel ACE inhibitory peptide from whey protein hydrolysate","volume":"130","author":"Pan","year":"2012","journal-title":"Food Chem."},{"key":"ref_42","doi-asserted-by":"crossref","unstructured":"Jakubczyk, A., and Baraniak, B. (2014). Angiotensin I converting enzyme inhibitory peptides obtained after in vitro hydrolysis of pea (Pisum sativum var Bajka) globulins. BioMed. Res. Int., 2014.","DOI":"10.1155\/2014\/438459"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"3573","DOI":"10.1007\/s00216-018-0925-x","article-title":"Peptidomic strategy for purification and identification of potential ACE-inhibitory and antioxidant peptides in Tetradesmus obliquus microalgae","volume":"410","author":"Montone","year":"2018","journal-title":"Anal. Bioanal. Chem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"12711","DOI":"10.1039\/D0RA00093K","article-title":"Karnchanatat Two novel ACE inhibitory peptides isolated from longan seeds: Purification, inhibitory kinetics and mechanisms","volume":"10","author":"Nuchprapha","year":"2020","journal-title":"RSC Adv."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"1197","DOI":"10.1007\/s10811-012-9913-2","article-title":"Enzyme proteolysis enhanced extraction of ACE inhibitory and antioxidant compounds (peptides and polyphenols) from Porphyra columbina residual cake","volume":"25","author":"Cian","year":"2013","journal-title":"J. Appl. Phycol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"696","DOI":"10.1016\/j.jfda.2017.07.008","article-title":"Production of antioxidant and ACE-inhibitory peptides from Kluyveromyces marxianus protein hydrolysates: Purification and molecular docking","volume":"26","author":"Mirzaei","year":"2018","journal-title":"J. Food Drug Anal."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.peptides.2014.07.026","article-title":"A novel angiotensin-I converting enzyme (ACE) inhibitory peptide from gastrointestinal protease hydrolysate of silkworm pupa (Bombyx mori) protein: Biochemical characterization and molecular docking study","volume":"68","author":"Wu","year":"2015","journal-title":"Peptides"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.jprot.2015.07.008","article-title":"Proteomics approach to examine the cardiotoxic effects of Nemopilema nomurai Jellyfish venom","volume":"128","author":"Choudhary","year":"2015","journal-title":"J. Proteom."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/j.toxlet.2020.10.012","article-title":"Danio rerio as an alternative vertebrate model for jellyfish venom study: The toxinological aspects of Nemopilema nomurai venom","volume":"335","author":"Prakash","year":"2020","journal-title":"Toxicol. Lett."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"112825","DOI":"10.1016\/j.lwt.2021.112825","article-title":"Enzymes-dependent antioxidant activity of sweet apricot kernel protein hydrolysates","volume":"154","author":"Huang","year":"2022","journal-title":"LWT"},{"key":"ref_52","unstructured":"Kit-WST, D.A. (2013). Technical Manual, Dojindo Molecular Technologies."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"107126","DOI":"10.1016\/j.toxicon.2023.107126","article-title":"Identification of cardiorespiratory toxic components of Nemopilema nomurai jellyfish venom using sequential chromatography methods","volume":"229","author":"Prakash","year":"2023","journal-title":"Toxicon"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.jprot.2017.03.003","article-title":"Functional proteomic analyses of Bothrops atrox venom reveals 635 phenotypes associated with habitat variation in the Amazon","volume":"159","author":"Sousa","year":"2017","journal-title":"J. Proteom."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1572","DOI":"10.1021\/jf1039876","article-title":"Analysis of the effect of temperature changes combined with different alkaline pH on the \u03b2-lactoglobulin trypsin hydrolysis pattern using MALDI-TOF-MS\/MS","volume":"59","author":"Cheison","year":"2011","journal-title":"J. Agric. Food Chem."},{"key":"ref_56","unstructured":"(2024, March 03). AlphaFold2.Ipynb\u2014Colaboratory. Available online: https:\/\/colab.research.google.com\/github\/sokrypton\/ColabFold\/blob\/main\/AlphaFold2.ipynb."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1038\/s41592-022-01488-1","article-title":"ColabFold: Making protein folding accessible to all","volume":"19","author":"Mirdita","year":"2022","journal-title":"Nat. Methods"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1691","DOI":"10.1016\/j.procbio.2014.06.021","article-title":"ACE inhibitory, hypotensive and antioxidant peptide fractions from Mucuna pruriens proteins","volume":"49","author":"Ruiz","year":"2014","journal-title":"Process Biochem."},{"key":"ref_59","doi-asserted-by":"crossref","unstructured":"Asirvatham, R.D., Hwang, D.H., Prakash, R.L.M., Kang, C., and Kim, E. (2023). Pharmacoinformatic Investigation of Silymarin as a Potential Inhibitor against Nemopilema nomurai Jellyfish Metalloproteinase Toxin-like Protein. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms24108972"}],"container-title":["Toxins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6651\/16\/9\/410\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T16:01:14Z","timestamp":1760112074000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6651\/16\/9\/410"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,9,20]]},"references-count":59,"journal-issue":{"issue":"9","published-online":{"date-parts":[[2024,9]]}},"alternative-id":["toxins16090410"],"URL":"https:\/\/doi.org\/10.3390\/toxins16090410","relation":{},"ISSN":["2072-6651"],"issn-type":[{"value":"2072-6651","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,9,20]]}}}