{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T21:57:37Z","timestamp":1788299857013,"version":"build-2803163510"},"reference-count":49,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2018,10,1]],"date-time":"2018-10-01T00:00:00Z","timestamp":1538352000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001807","name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado de S\u00e3o Paulo","doi-asserted-by":"publisher","award":["2009\/07128-7 and 2011\/21031-6"],"award-info":[{"award-number":["2009\/07128-7 and 2011\/21031-6"]}],"id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001807","name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado de S\u00e3o Paulo","doi-asserted-by":"publisher","award":["2016\/17951-6 and 2016\/13368-4"],"award-info":[{"award-number":["2016\/17951-6 and 2016\/13368-4"]}],"id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","award":["142066\/2014-1"],"award-info":[{"award-number":["142066\/2014-1"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Marine Drugs"],"abstract":"<jats:p>Voltage-gated potassium (KV) channels regulate diverse physiological processes and are an important target for developing novel therapeutic approaches. Sea anemone (Cnidaria, Anthozoa) venoms comprise a highly complex mixture of peptide toxins with diverse and selective pharmacology on KV channels. From the nematocysts of the sea anemone Actinia bermudensis, a peptide that we named AbeTx1 was purified and functionally characterized on 12 different subtypes of KV channels (KV1.1\u2013KV1.6; KV2.1; KV3.1; KV4.2; KV4.3; KV11.1; and, Shaker IR), and three voltage-gated sodium channel isoforms (NaV1.2, NaV1.4, and BgNaV). AbeTx1 was selective for Shaker-related K+ channels and is capable of inhibiting K+ currents, not only by blocking the K+ current of KV1.2 subtype, but by altering the energetics of activation of KV1.1 and KV1.6. Moreover, experiments using six synthetic alanine point-mutated analogs further showed that a ring of basic amino acids acts as a multipoint interaction for the binding of the toxin to the channel. The AbeTx1 primary sequence is composed of 17 amino acids with a high proportion of lysines and arginines, including two disulfide bridges (Cys1\u2013Cys4 and Cys2\u2013Cys3), and it is devoid of aromatic or aliphatic amino acids. Secondary structure analysis reveals that AbeTx1 has a highly flexible, random-coil-like conformation, but with a tendency of structuring in the beta sheet. Its overall structure is similar to open-ended cyclic peptides found on the scorpion \u03ba-KTx toxins family, cone snail venoms, and antimicrobial peptides.<\/jats:p>","DOI":"10.3390\/md16100360","type":"journal-article","created":{"date-parts":[[2018,10,2]],"date-time":"2018-10-02T08:23:50Z","timestamp":1538468630000},"page":"360","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["AbeTx1 Is a Novel Sea Anemone Toxin with a Dual Mechanism of Action on Shaker-Type K+ Channels Activation"],"prefix":"10.3390","volume":"16","author":[{"given":"Diego J.","family":"B. Orts","sequence":"first","affiliation":[{"name":"Department of Physiology, Institute of Biosciences, University of S\u00e3o Paulo, 05508-090 S\u00e3o Paulo, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0504-5702","authenticated-orcid":false,"given":"Steve","family":"Peigneur","sequence":"additional","affiliation":[{"name":"Toxicology and Pharmacology, University of Leuven (KU Leuven), Campus Gasthuisberg O&amp;N2, Herestraat 49, P.O. Box 922, 3000 Leuven, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"La\u00edz Costa","family":"Silva-Gon\u00e7alves","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Neurobiologia Estrutural e Funcional (LaNEF), Departamento de Biof\u00edsica, Universidade Federal de S\u00e3o Paulo, 04023-062 S\u00e3o Paulo, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1086-086X","authenticated-orcid":false,"given":"Manoel","family":"Arcisio-Miranda","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Neurobiologia Estrutural e Funcional (LaNEF), Departamento de Biof\u00edsica, Universidade Federal de S\u00e3o Paulo, 04023-062 S\u00e3o Paulo, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jos\u00e9 Eduardo","family":"P. W. Bicudo","sequence":"additional","affiliation":[{"name":"Department of Physiology, Institute of Biosciences, University of S\u00e3o Paulo, 05508-090 S\u00e3o Paulo, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jan","family":"Tytgat","sequence":"additional","affiliation":[{"name":"Toxicology and Pharmacology, University of Leuven (KU Leuven), Campus Gasthuisberg O&amp;N2, Herestraat 49, P.O. Box 922, 3000 Leuven, Belgium"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2018,10,1]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1124\/pr.55.4.9","article-title":"International union of pharmacology. XLI. compendium of voltage-gated ion channels: Potassium channels","volume":"55","author":"Gutman","year":"2003","journal-title":"Pharmacol. 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