{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T14:31:49Z","timestamp":1792506709792,"version":"4.5.0"},"reference-count":49,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2025,2,21]],"date-time":"2025-02-21T00:00:00Z","timestamp":1740096000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100006769","name":"Russian Science Foundation","doi-asserted-by":"publisher","award":["22-75-10021"],"award-info":[{"award-number":["22-75-10021"]}],"id":[{"id":"10.13039\/501100006769","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>Mambalgins are peptide inhibitors of acid-sensing ion channels type 1 (ASIC1) with potent analgesic effects in models of inflammatory and neuropathic pain. To optimize recombinant peptide production and enhance pharmacological properties, we developed a mutant analog of mambalgin-1 (Mamb) through molecular modeling and site-directed mutagenesis. The resulting peptide, Mamb-AL, features methionine-to-alanine and methionine-to-leucine substitutions, allowing for a more efficient recombinant production protocol in E. coli. Electrophysiological experiments demonstrated that Mamb-AL exhibits three-fold and five-fold greater inhibition of homomeric ASIC1a and ASIC1b channels, respectively, and a two-fold increase in inhibition of heteromeric ASIC1a\/3 channels compared with Mamb. In a mouse model of acetic acid-induced writhing pain, Mamb-AL showed a trend toward stronger analgesic efficacy than the wild-type peptide. These improvements in both production efficiency and pharmacological properties make Mamb-AL a valuable tool for studying ASIC channels and a promising candidate for analgesic drug development.<\/jats:p>","DOI":"10.3390\/toxins17030101","type":"journal-article","created":{"date-parts":[[2025,2,21]],"date-time":"2025-02-21T10:12:11Z","timestamp":1740132731000},"page":"101","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Two Amino Acid Substitutions Improve the Pharmacological Profile of the Snake Venom Peptide Mambalgin"],"prefix":"10.3390","volume":"17","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6588-5012","authenticated-orcid":false,"given":"Dmitry I.","family":"Osmakov","sequence":"first","affiliation":[{"name":"Shemyakin\u2014Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Ul. Miklukho-Maklaya 16\/10, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0002-1444-3665","authenticated-orcid":false,"given":"Timur A.","family":"Khasanov","sequence":"additional","affiliation":[{"name":"Shemyakin\u2014Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Ul. Miklukho-Maklaya 16\/10, 117997 Moscow, Russia"},{"name":"Moscow Center for Advanced Studies, Kulakova Str. 20, 123592 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ekaterina E.","family":"Maleeva","sequence":"additional","affiliation":[{"name":"Shemyakin\u2014Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Ul. Miklukho-Maklaya 16\/10, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0003-8949-5600","authenticated-orcid":false,"given":"Vladimir M.","family":"Pavlov","sequence":"additional","affiliation":[{"name":"Branch of the Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 6 Nauki Avenue, 142290 Pushchino, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2989-4477","authenticated-orcid":false,"given":"Victor A.","family":"Palikov","sequence":"additional","affiliation":[{"name":"Branch of the Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 6 Nauki Avenue, 142290 Pushchino, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5603-5371","authenticated-orcid":false,"given":"Olga A.","family":"Belozerova","sequence":"additional","affiliation":[{"name":"Shemyakin\u2014Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Ul. Miklukho-Maklaya 16\/10, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sergey G.","family":"Koshelev","sequence":"additional","affiliation":[{"name":"Shemyakin\u2014Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Ul. Miklukho-Maklaya 16\/10, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8556-5366","authenticated-orcid":false,"given":"Yuliya V.","family":"Korolkova","sequence":"additional","affiliation":[{"name":"Shemyakin\u2014Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Ul. Miklukho-Maklaya 16\/10, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3053-2804","authenticated-orcid":false,"given":"Igor A.","family":"Dyachenko","sequence":"additional","affiliation":[{"name":"Branch of the Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 6 Nauki Avenue, 142290 Pushchino, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0242-4240","authenticated-orcid":false,"given":"Sergey A.","family":"Kozlov","sequence":"additional","affiliation":[{"name":"Shemyakin\u2014Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Ul. Miklukho-Maklaya 16\/10, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7628-0980","authenticated-orcid":false,"given":"Yaroslav A.","family":"Andreev","sequence":"additional","affiliation":[{"name":"Shemyakin\u2014Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Ul. Miklukho-Maklaya 16\/10, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,2,21]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"2671","DOI":"10.1111\/bph.13533","article-title":"The function and regulation of acid-sensing ion channels (ASICs) and the epithelial Na+ channel (ENaC): IUPHAR Review 19","volume":"173","author":"Boscardin","year":"2016","journal-title":"Br. J. Pharmacol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"C699","DOI":"10.1152\/ajpcell.00188.2012","article-title":"Structure and activity of the acid-sensing ion channels","volume":"303","author":"Sherwood","year":"2012","journal-title":"Am. J. Physiol. Physiol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1124\/pr.114.009225","article-title":"International union of basic and clinical pharmacology. XCI. Structure, function, and pharmacology of acid-sensing ion channels and the epithelial Na+ channel","volume":"67","author":"Kellenberger","year":"2015","journal-title":"Pharmacol. Rev."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"316","DOI":"10.1038\/nature06163","article-title":"Structure of acid-sensing ion channel 1 at 1.9 \u00c5 resolution and low pH","volume":"449","author":"Jasti","year":"2007","journal-title":"Nature"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1038\/nature08218","article-title":"Pore architecture and ion sites in acid-sensing ion channels and P2X receptors","volume":"460","author":"Gonzales","year":"2009","journal-title":"Nature"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1016\/j.cell.2014.01.011","article-title":"X-Ray Structure of acid-sensing ion channel 1-snake toxin complex reveals open state of a Na+-selective channel","volume":"156","author":"Baconguis","year":"2014","journal-title":"Cell"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1038\/nature25782","article-title":"Gating mechanisms of acid-sensing ion channels","volume":"555","author":"Yoder","year":"2018","journal-title":"Nature"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/j.neuropharm.2015.02.009","article-title":"Acid-sensing ion channels and nociception in the peripheral and central nervous systems","volume":"94","author":"Deval","year":"2015","journal-title":"Neuropharmacology"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"1083","DOI":"10.1038\/nn.3750","article-title":"Acid-sensing ion channels contribute to synaptic transmission and inhibit cocaine-evoked plasticity","volume":"17","author":"Kreple","year":"2014","journal-title":"Nat. Neurosci."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1016\/S0896-6273(02)00661-X","article-title":"The acid-activated ion channel ASIC contributes to synaptic plasticity, learning, and memory","volume":"34","author":"Wemmie","year":"2002","journal-title":"Neuron"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1111\/gbb.12398","article-title":"ASIC1A in neurons is critical for fear-related behaviors","volume":"16","author":"Taugher","year":"2017","journal-title":"Genes Brain Behav."},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Kalinovskii, A.P., Pushkarev, A.P., Mikhailenko, A.D., Kudryavtsev, D.S., Belozerova, O.A., Shmygarev, V.I., Yatskin, O.N., Korolkova, Y.V., Kozlov, S.A., and Osmakov, D.I. (2023). Dual modulator of ASIC channels and GABAA receptors from thyme alters fear-related hippocampal activity. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms241713148"},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Aissouni, Y., El Guerrab, A., Hamieh, A.M., Ferrier, J., Chalus, M., Lemaire, D., Gr\u00e9goire, S., Etienne, M., Eschalier, A., and Ardid, D. (2017). Acid-sensing ion channel 1a in the amygdala is involved in pain and anxiety-related behaviours associated with arthritis. Sci. Rep., 7.","DOI":"10.1038\/srep43617"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"826","DOI":"10.1038\/s41586-024-07684-7","article-title":"Glutamate acts on acid-sensing ion channels to worsen ischaemic brain injury","volume":"631","author":"Lai","year":"2024","journal-title":"Nature"},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Gobetto, M.N., Castellanos, L.C.S., Contreras, N.E., Sodero, A.O., Cambiagno, D.A., Malnati, G.O.M., Montes, M.M., Uchitel, O.D., and Weissmann, C. (2022). Segmental upregulation of ASIC1 channels in the formalin acute pain mouse model. Pharmaceuticals, 15.","DOI":"10.3390\/ph15121539"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1035","DOI":"10.1016\/j.tips.2021.09.008","article-title":"Acid-sensing ion channels as potential therapeutic targets","volume":"42","author":"Heusser","year":"2021","journal-title":"Trends Pharmacol. Sci."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1571","DOI":"10.1093\/eurheartj\/ehad793","article-title":"Acid-sensing ion channel 1a blockade reduces myocardial injury in rodent models of myocardial infarction","volume":"45","author":"Redd","year":"2024","journal-title":"Eur. Heart J."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"e38031","DOI":"10.1016\/j.heliyon.2024.e38031","article-title":"Pathology and physiology of acid-sensitive ion channels in the bladder","volume":"10","author":"Zhang","year":"2024","journal-title":"Heliyon"},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Osmakov, D.I., Khasanov, T.A., Andreev, Y.A., Lyukmanova, E.N., and Kozlov, S.A. (2020). Animal, herb, and microbial toxins for structural and pharmacological study of acid-sensing ion channels. Front. Pharmacol., 11.","DOI":"10.3389\/fphar.2020.00991"},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Verkest, C., Salinas, M., Diochot, S., Deval, E., Lingueglia, E., and Baron, A. (2022). Mechanisms of action of the peptide toxins targeting human and rodent acid-sensing ion channels and relevance to their in vivo analgesic effects. Toxins, 14.","DOI":"10.3390\/toxins14100709"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1038\/nature11494","article-title":"Black mamba venom peptides target acid-sensing ion channels to abolish pain","volume":"490","author":"Diochot","year":"2012","journal-title":"Nature"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"e2021581118","DOI":"10.1073\/pnas.2021581118","article-title":"Mambalgin-3 potentiates human acid-sensing ion channel 1b under mild to moderate acidosis: Implications as an analgesic lead","volume":"118","author":"Budusan","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1038\/s41421-018-0026-1","article-title":"Cryo-EM structure of the ASIC1a\u2013mambalgin-1 complex reveals that the peptide toxin mambalgin-1 inhibits acid-sensing ion channels through an unusual allosteric effect","volume":"4","author":"Sun","year":"2018","journal-title":"Cell Discov."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"e57096","DOI":"10.7554\/eLife.57096","article-title":"Structural insights into human acid-sensing ion channel 1a inhibition by snake toxin mambalgin1","volume":"9","author":"Sun","year":"2020","journal-title":"Elife"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1002\/anie.201308898","article-title":"Chemical synthesis, 3D structure, and ASIC binding site of the toxin mambalgin-2","volume":"53","author":"Schroeder","year":"2014","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"108453","DOI":"10.1016\/j.neuropharm.2021.108453","article-title":"Mambalgin-1 pain-relieving peptide locks the hinge between \u03b14 and \u03b15 helices to inhibit rat acid-sensing ion channel 1a","volume":"185","author":"Salinas","year":"2021","journal-title":"Neuropharmacology"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1007\/s00018-024-05276-2","article-title":"Revealing molecular determinants governing mambalgin-3 pharmacology at acid-sensing ion channel 1 variants","volume":"81","author":"Budusan","year":"2024","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1097\/j.pain.0000000000000397","article-title":"Analgesic effects of mambalgin peptide inhibitors of acid-sensing ion channels in inflammatory and neuropathic pain","volume":"157","author":"Diochot","year":"2016","journal-title":"Pain"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"4154","DOI":"10.1111\/bph.14462","article-title":"Effects of systemic inhibitors of acid-sensing ion channels 1 (ASIC1) against acute and chronic mechanical allodynia in a rodent model of migraine","volume":"175","author":"Verkest","year":"2018","journal-title":"Br. J. Pharmacol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"13363","DOI":"10.1074\/jbc.M114.561076","article-title":"Binding site and inhibitory mechanism of the mambalgin-2 pain-relieving peptide on acid-sensing ion channel 1a","volume":"289","author":"Salinas","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"2616","DOI":"10.1074\/jbc.M115.702373","article-title":"Mambalgin-1 pain-relieving peptide, stepwise solid-phase synthesis, crystal structure, and functional domain for acid-sensing ion channel 1a inhibition","volume":"291","author":"Mourier","year":"2016","journal-title":"J. Biol. Chem."},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Bychkov, M., Shulepko, M., Osmakov, D., Andreev, Y., Sudarikova, A., Vasileva, V., Pavlyukov, M.S., Latyshev, Y.A., Potapov, A.A., and Kirpichnikov, M. (2020). Mambalgin-2 induces cell cycle arrest and apoptosis in glioma cells via interaction with ASIC1a. Cancers, 12.","DOI":"10.3390\/cancers12071837"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1186\/s12934-024-02316-1","article-title":"Scalable production of recombinant three-finger proteins: From inclusion bodies to high quality molecular probes","volume":"23","author":"Xu","year":"2024","journal-title":"Microb. Cell Fact."},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Gasteiger, E., Hoogland, C., Gattiker, A., Duvaud, S., Wilkins, M.R., Appel, R.D., and Bairoch, A. (2005). Protein identification and analysis tools on the ExPASy server. The Proteomics Protocols Handbook, Humana Press.","DOI":"10.1385\/1-59259-890-0:571"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"3285","DOI":"10.1074\/mcp.M113.030437","article-title":"Selective targeting of the cysteine proteome by thioredoxin and glutathione redox systems","volume":"12","author":"Go","year":"2013","journal-title":"Mol. Cell. Proteom."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1016\/j.mencom.2020.03.028","article-title":"Refolding of disulfide containing peptides in fusion with thioredoxin","volume":"30","author":"Logashina","year":"2020","journal-title":"Mendeleev Commun."},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Chang, C.-T., Fong, S.W., Lee, C.-H., Chuang, Y.-C., Lin, S.-H., and Chen, C.-C. (2019). Involvement of acid-sensing ion channel 1b in the development of acid-induced chronic muscle pain. Front. Neurosci., 13.","DOI":"10.3389\/fnins.2019.01247"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"1411","DOI":"10.3390\/ph3051411","article-title":"Acid-sensing ion channels and pain","volume":"3","author":"Gu","year":"2010","journal-title":"Pharmaceuticals"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1016\/j.toxicon.2010.07.010","article-title":"Structure, function and evolution of three-finger toxins: Mini proteins with multiple targets","volume":"56","author":"Kini","year":"2010","journal-title":"Toxicon"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"17","DOI":"10.4331\/wjbc.v10.i1.17","article-title":"Last decade update for three-finger toxins: Newly emerging structures and biological activities","volume":"10","author":"Utkin","year":"2019","journal-title":"World J. Biol. Chem."},{"key":"ref_41","doi-asserted-by":"crossref","unstructured":"Kalinovskii, A.P., Osmakov, D.I., Koshelev, S.G., Lubova, K.I., Korolkova, Y.V., Kozlov, S.A., and Andreev, Y.A. (2022). Retinoic acid-differentiated neuroblastoma SH-SY5Y is an accessible in vitro model to study native human acid-sensing ion channels 1a (ASIC1a). Biology, 11.","DOI":"10.3390\/biology11020167"},{"key":"ref_42","doi-asserted-by":"crossref","unstructured":"Osmakov, D.I., Koshelev, S.G., Lyukmanova, E.N., Shulepko, M.A., Andreev, Y.A., Illes, P., and Kozlov, S.A. (2019). Multiple modulation of acid-sensing ion channel 1a by the alkaloid daurisoline. Biomolecules, 9.","DOI":"10.3390\/biom9080336"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"1530","DOI":"10.1038\/mt.2014.86","article-title":"Characterizing human stem cell\u2013derived sensory neurons at the single-cell level reveals their ion channel expression and utility in pain research","volume":"22","author":"Young","year":"2014","journal-title":"Mol. Ther."},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Chaudhary, K., Kumar, R., Singh, S., Tuknait, A., Gautam, A., Mathur, D., Anand, P., Varshney, G.C., and Raghava, G.P.S. (2016). A Web server and mobile app for computing hemolytic potency of peptides. Sci. Rep., 6.","DOI":"10.1038\/srep22843"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1038\/s41514-017-0013-z","article-title":"How does hormesis impact biology, toxicology, and medicine?","volume":"3","author":"Calabrese","year":"2017","journal-title":"NPJ Aging Mech. Dis."},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Andreev, Y., Osmakov, D., Koshelev, S., Maleeva, E., Logashina, Y., Palikov, V., Palikova, Y., Dyachenko, I., and Kozlov, S. (2018). Analgesic activity of acid-sensing ion channel 3 (ASIC3) inhibitors: Sea anemones peptides Ugr9-1 and APETx2 versus low molecular weight compounds. Mar. Drugs, 16.","DOI":"10.3390\/md16120500"},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Khasanov, T.A., Maleeva, E.E., Koshelev, S.G., Palikov, V.A., Palikova, Y.A., Dyachenko, I.A., Kozlov, S.A., Andreev, Y.A., and Osmakov, D.I. (2024). Mutagenesis of the peptide inhibitor of ASIC3 channel introduces binding to thumb domain of ASIC1a but reduces analgesic activity. Mar. Drugs, 22.","DOI":"10.3390\/md22090382"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"W233","DOI":"10.1093\/nar\/gkn216","article-title":"The RosettaDock server for local protein-protein docking","volume":"36","author":"Lyskov","year":"2008","journal-title":"Nucleic Acids Res."},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Osmakov, D.I., Koshelev, S.G., Palikov, V.A., Palikova, Y.A., Shaykhutdinova, E.R., Dyachenko, I.A., Andreev, Y.A., and Kozlov, S.A. (2019). Alkaloid lindoldhamine inhibits acid-sensing ion channel 1a and reveals anti-inflammatory properties. Toxins, 11.","DOI":"10.3390\/toxins11090542"}],"container-title":["Toxins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6651\/17\/3\/101\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,9]],"date-time":"2025-10-09T16:40:01Z","timestamp":1760028001000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6651\/17\/3\/101"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,2,21]]},"references-count":49,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2025,3]]}},"alternative-id":["toxins17030101"],"URL":"https:\/\/doi.org\/10.3390\/toxins17030101","relation":{},"ISSN":["2072-6651"],"issn-type":[{"value":"2072-6651","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,2,21]]}}}