Revisiting cangitoxin, a sea anemone peptide: Purification and characterization of cangitoxins II and III from the venom of Bunodosoma cangicum
Sodium channel toxins from sea anemones are employed as tools for dissecting the biophysical properties of inactivation in voltage-gated sodium channels. Cangitoxin (CGTX) is a peptide containing 48 amino acid residues and was formerly purified from Bunodosoma cangicum. Nevertheless, previous works...
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| Veröffentlicht in: | Toxicon (Oxford) 2008-06, Vol.51 (7), p.1303-1307 |
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| container_title | Toxicon (Oxford) |
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| creator | Zaharenko, André Junqueira Ferreira, Wilson Alves de Oliveira, Joacir Stolarz Konno, Katsuhiro Richardson, Michael Schiavon, Emanuele Wanke, Enzo de Freitas, José Carlos |
| description | Sodium channel toxins from sea anemones are employed as tools for dissecting the biophysical properties of inactivation in voltage-gated sodium channels. Cangitoxin (CGTX) is a peptide containing 48 amino acid residues and was formerly purified from
Bunodosoma cangicum. Nevertheless, previous works reporting the isolation procedures for such peptide from
B. cangicum secretions are controversial and may lead to incorrect information. In this paper, we report a simple and rapid procedure, consisting of two chromatographic steps, in order to obtain a CGTX analog directly from sea anemone venom. We also report a substitution of N16D in this peptide sample and the co-elution of an inseparable minor isoform presenting the R14H substitution. Peptides are named as CGTX-II and CGTX-III, and their effects over Nav1.1 channels in patch clamp experiments are demonstrated. |
| doi_str_mv | 10.1016/j.toxicon.2008.01.011 |
| format | Article |
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Bunodosoma cangicum. Nevertheless, previous works reporting the isolation procedures for such peptide from
B. cangicum secretions are controversial and may lead to incorrect information. In this paper, we report a simple and rapid procedure, consisting of two chromatographic steps, in order to obtain a CGTX analog directly from sea anemone venom. We also report a substitution of N16D in this peptide sample and the co-elution of an inseparable minor isoform presenting the R14H substitution. Peptides are named as CGTX-II and CGTX-III, and their effects over Nav1.1 channels in patch clamp experiments are demonstrated.</description><identifier>ISSN: 0041-0101</identifier><identifier>EISSN: 1879-3150</identifier><identifier>DOI: 10.1016/j.toxicon.2008.01.011</identifier><identifier>PMID: 18342901</identifier><identifier>CODEN: TOXIA6</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Amino Acid Sequence ; Animal poisons toxicology. Antivenoms ; Animals ; Biological and medical sciences ; Bunodosoma cangicum ; Cangitoxin ; Cells, Cultured ; Chemical Fractionation ; Cnidarian Venoms - chemistry ; Cnidarian Venoms - toxicity ; Edman sequencing ; Ganglia, Spinal - drug effects ; Ganglia, Spinal - physiology ; HPLC ; Humans ; Marine ; Medical sciences ; Molecular Sequence Data ; Neurotoxins - chemistry ; Neurotoxins - toxicity ; Patch clamp ; Patch-Clamp Techniques ; Peptide Fragments - chemistry ; Protein Isoforms ; Rats ; Rats, Wistar ; Sea anemone ; Sea Anemones ; Sodium Channels - drug effects ; Structure-Activity Relationship ; Toxicology</subject><ispartof>Toxicon (Oxford), 2008-06, Vol.51 (7), p.1303-1307</ispartof><rights>2008 Elsevier Ltd</rights><rights>2008 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c424t-cede5e0106495025b42795e944a5372862a92371765d467ee4ae81c6e6ad1cbe3</citedby><cites>FETCH-LOGICAL-c424t-cede5e0106495025b42795e944a5372862a92371765d467ee4ae81c6e6ad1cbe3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.toxicon.2008.01.011$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20435217$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18342901$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zaharenko, André Junqueira</creatorcontrib><creatorcontrib>Ferreira, Wilson Alves</creatorcontrib><creatorcontrib>de Oliveira, Joacir Stolarz</creatorcontrib><creatorcontrib>Konno, Katsuhiro</creatorcontrib><creatorcontrib>Richardson, Michael</creatorcontrib><creatorcontrib>Schiavon, Emanuele</creatorcontrib><creatorcontrib>Wanke, Enzo</creatorcontrib><creatorcontrib>de Freitas, José Carlos</creatorcontrib><title>Revisiting cangitoxin, a sea anemone peptide: Purification and characterization of cangitoxins II and III from the venom of Bunodosoma cangicum</title><title>Toxicon (Oxford)</title><addtitle>Toxicon</addtitle><description>Sodium channel toxins from sea anemones are employed as tools for dissecting the biophysical properties of inactivation in voltage-gated sodium channels. Cangitoxin (CGTX) is a peptide containing 48 amino acid residues and was formerly purified from
Bunodosoma cangicum. Nevertheless, previous works reporting the isolation procedures for such peptide from
B. cangicum secretions are controversial and may lead to incorrect information. In this paper, we report a simple and rapid procedure, consisting of two chromatographic steps, in order to obtain a CGTX analog directly from sea anemone venom. We also report a substitution of N16D in this peptide sample and the co-elution of an inseparable minor isoform presenting the R14H substitution. Peptides are named as CGTX-II and CGTX-III, and their effects over Nav1.1 channels in patch clamp experiments are demonstrated.</description><subject>Amino Acid Sequence</subject><subject>Animal poisons toxicology. Antivenoms</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Bunodosoma cangicum</subject><subject>Cangitoxin</subject><subject>Cells, Cultured</subject><subject>Chemical Fractionation</subject><subject>Cnidarian Venoms - chemistry</subject><subject>Cnidarian Venoms - toxicity</subject><subject>Edman sequencing</subject><subject>Ganglia, Spinal - drug effects</subject><subject>Ganglia, Spinal - physiology</subject><subject>HPLC</subject><subject>Humans</subject><subject>Marine</subject><subject>Medical sciences</subject><subject>Molecular Sequence Data</subject><subject>Neurotoxins - chemistry</subject><subject>Neurotoxins - toxicity</subject><subject>Patch clamp</subject><subject>Patch-Clamp Techniques</subject><subject>Peptide Fragments - chemistry</subject><subject>Protein Isoforms</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Sea anemone</subject><subject>Sea Anemones</subject><subject>Sodium Channels - drug effects</subject><subject>Structure-Activity Relationship</subject><subject>Toxicology</subject><issn>0041-0101</issn><issn>1879-3150</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkduKFDEQhoMo7uzqIyi50avtsSqdPnmz6OJhYEERvQ6ZdPVuhulkTNKD-hK-shm7Ue-EggrJ91el6mfsCcIaAesXu3Xy36zxbi0A2jVgDrzHVtg2XVFiBffZCkBiARk_Y-cx7gCgbLv6ITvDtpSiA1yxn5_oaKNN1t1yo92tPVV1l1zzSJprR6N3xA90SLanl_zjFOxgjU7Wu_zac3OngzaJgv0xX_rhnzqRbza_sU3OQ_AjT3fEj-TyKYOvJ-d7H_2oZ42ZxkfswaD3kR4v-YJ9efvm8_X74ubDu831q5vCSCFTYainivJotewqENVWiqarqJNSV2Uj2lroTpQNNnXVy7ohkppaNDXVukezpfKCPZ_rHoL_OlFMarTR0H6fR_ZTVAKwa0ULGaxm0AQfY6BBHYIddfiuENTJCbVTixPq5IQCzIFZ93RpMG1H6v-qltVn4NkC6Gj0fgjaGRv_cAJkWQlsMnc1c5TXcbQUVDSWXN6ADWSS6r39z1d-AYjCq00</recordid><startdate>20080601</startdate><enddate>20080601</enddate><creator>Zaharenko, André Junqueira</creator><creator>Ferreira, Wilson Alves</creator><creator>de Oliveira, Joacir Stolarz</creator><creator>Konno, Katsuhiro</creator><creator>Richardson, Michael</creator><creator>Schiavon, Emanuele</creator><creator>Wanke, Enzo</creator><creator>de Freitas, José Carlos</creator><general>Elsevier Ltd</general><general>Elsevier Science</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TN</scope><scope>7U7</scope><scope>C1K</scope><scope>F1W</scope><scope>H95</scope><scope>H97</scope><scope>L.G</scope></search><sort><creationdate>20080601</creationdate><title>Revisiting cangitoxin, a sea anemone peptide: Purification and characterization of cangitoxins II and III from the venom of Bunodosoma cangicum</title><author>Zaharenko, André Junqueira ; Ferreira, Wilson Alves ; de Oliveira, Joacir Stolarz ; Konno, Katsuhiro ; Richardson, Michael ; Schiavon, Emanuele ; Wanke, Enzo ; de Freitas, José Carlos</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c424t-cede5e0106495025b42795e944a5372862a92371765d467ee4ae81c6e6ad1cbe3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Amino Acid Sequence</topic><topic>Animal poisons toxicology. Antivenoms</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Bunodosoma cangicum</topic><topic>Cangitoxin</topic><topic>Cells, Cultured</topic><topic>Chemical Fractionation</topic><topic>Cnidarian Venoms - chemistry</topic><topic>Cnidarian Venoms - toxicity</topic><topic>Edman sequencing</topic><topic>Ganglia, Spinal - drug effects</topic><topic>Ganglia, Spinal - physiology</topic><topic>HPLC</topic><topic>Humans</topic><topic>Marine</topic><topic>Medical sciences</topic><topic>Molecular Sequence Data</topic><topic>Neurotoxins - chemistry</topic><topic>Neurotoxins - toxicity</topic><topic>Patch clamp</topic><topic>Patch-Clamp Techniques</topic><topic>Peptide Fragments - chemistry</topic><topic>Protein Isoforms</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Sea anemone</topic><topic>Sea Anemones</topic><topic>Sodium Channels - drug effects</topic><topic>Structure-Activity Relationship</topic><topic>Toxicology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zaharenko, André Junqueira</creatorcontrib><creatorcontrib>Ferreira, Wilson Alves</creatorcontrib><creatorcontrib>de Oliveira, Joacir Stolarz</creatorcontrib><creatorcontrib>Konno, Katsuhiro</creatorcontrib><creatorcontrib>Richardson, Michael</creatorcontrib><creatorcontrib>Schiavon, Emanuele</creatorcontrib><creatorcontrib>Wanke, Enzo</creatorcontrib><creatorcontrib>de Freitas, José Carlos</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Oceanic Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 3: Aquatic Pollution & Environmental Quality</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><jtitle>Toxicon (Oxford)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zaharenko, André Junqueira</au><au>Ferreira, Wilson Alves</au><au>de Oliveira, Joacir Stolarz</au><au>Konno, Katsuhiro</au><au>Richardson, Michael</au><au>Schiavon, Emanuele</au><au>Wanke, Enzo</au><au>de Freitas, José Carlos</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Revisiting cangitoxin, a sea anemone peptide: Purification and characterization of cangitoxins II and III from the venom of Bunodosoma cangicum</atitle><jtitle>Toxicon (Oxford)</jtitle><addtitle>Toxicon</addtitle><date>2008-06-01</date><risdate>2008</risdate><volume>51</volume><issue>7</issue><spage>1303</spage><epage>1307</epage><pages>1303-1307</pages><issn>0041-0101</issn><eissn>1879-3150</eissn><coden>TOXIA6</coden><abstract>Sodium channel toxins from sea anemones are employed as tools for dissecting the biophysical properties of inactivation in voltage-gated sodium channels. Cangitoxin (CGTX) is a peptide containing 48 amino acid residues and was formerly purified from
Bunodosoma cangicum. Nevertheless, previous works reporting the isolation procedures for such peptide from
B. cangicum secretions are controversial and may lead to incorrect information. In this paper, we report a simple and rapid procedure, consisting of two chromatographic steps, in order to obtain a CGTX analog directly from sea anemone venom. We also report a substitution of N16D in this peptide sample and the co-elution of an inseparable minor isoform presenting the R14H substitution. Peptides are named as CGTX-II and CGTX-III, and their effects over Nav1.1 channels in patch clamp experiments are demonstrated.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>18342901</pmid><doi>10.1016/j.toxicon.2008.01.011</doi><tpages>5</tpages></addata></record> |
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| subjects | Amino Acid Sequence Animal poisons toxicology. Antivenoms Animals Biological and medical sciences Bunodosoma cangicum Cangitoxin Cells, Cultured Chemical Fractionation Cnidarian Venoms - chemistry Cnidarian Venoms - toxicity Edman sequencing Ganglia, Spinal - drug effects Ganglia, Spinal - physiology HPLC Humans Marine Medical sciences Molecular Sequence Data Neurotoxins - chemistry Neurotoxins - toxicity Patch clamp Patch-Clamp Techniques Peptide Fragments - chemistry Protein Isoforms Rats Rats, Wistar Sea anemone Sea Anemones Sodium Channels - drug effects Structure-Activity Relationship Toxicology |
| title | Revisiting cangitoxin, a sea anemone peptide: Purification and characterization of cangitoxins II and III from the venom of Bunodosoma cangicum |
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