{"refrec":{"BRefID":238150,"RR":"<b>Bergeron, Z.L.; Chun, J.B.; Baker, M.R.; Sandall, D.W.; Peigneur, S.; Yu, P.Y.C.; Thapa, P.; Milisen, J.W.; Tytgat, J.; Livett, B.G.; Bingham, J.P.</b> (2013). A 'conovenomic' analysis of the milked venom from the mollusk-hunting cone snail <i>Conus textile</i>-The pharmacological importance of post-translational modifications. <i>Peptides (New York, NY : 1980) 49</i>: 145-158. <a href=\"http://dx.doi.org/10.1016/j.peptides.2013.09.004\" target=\"_blank\">dx.doi.org/10.1016/j.peptides.2013.09.004</a>","BEntID":229837,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>Peptides (New York, NY : 1980) 49</i>: 145-158. <a href=\"https://dx.doi.org/10.1016/j.peptides.2013.09.004\" target=\"_blank\">https://dx.doi.org/10.1016/j.peptides.2013.09.004</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":0,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Bergeron, Z.L.; Chun, J.B.; Baker, M.R.; Sandall, D.W.; Peigneur, S.; Yu, P.Y.C.; Thapa, P.; Milisen, J.W.; Tytgat, J.; Livett, B.G.; Bingham, J.P.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Bergeron, Z.L. <i>et al.</i>","Englishabstract":"Cone snail venoms provide a largely untapped source of novel peptide drug leads. To enhance the discovery phase, a detailed comparative proteomic analysis was undertaken on milked venom from the mollusk-hunting cone snail, <i>Conus textile</i>, from three different geographic locations (Hawai’i, American Samoa and Australia's Great Barrier Reef). A novel milked venom conopeptide rich in post-translational modifications was discovered, characterized and named a-conotoxin TxIC. We assign this conopeptide to the 4/7 a-conotoxin family based on the peptide's sequence homology and cDNA pre-propeptide alignment. Pharmacologically, a-conotoxin TxIC demonstrates minimal activity on human acetylcholine receptor models (100 µM, < 5% inhibition), compared to its high paralytic potency in invertebrates, PD<sub>50</sub> = 34.2 nMol kg<sup>-1</sup>. The non-post-translationally modified form, [Pro]<sup>2,8</sup>[Glu]<sup>16</sup>a-conotoxin TxIC, demonstrates differential selectivity for the a3ß2 isoform of the nicotinic acetylcholine receptor with maximal inhibition of 96% and an observed IC<sub>50</sub> of 5.4 ± 0.5 µM. Interestingly its comparative PD<sub>50</sub> (3.6 µMol kg<sup>-1</sup>) in invertebrates was ~100 fold more than that of the native peptide. Differentiating a-conotoxin TxIC from other a-conotoxins is the high degree of post-translational modification (44% of residues). This includes the incorporation of ?-carboxyglutamic acid, two moieties of 4-trans hydroxyproline, two disulfide bond linkages, and C-terminal amidation. These findings expand upon the known chemical diversity of a-conotoxins and illustrate a potential driver of toxin phyla-selectivity within <i>Conus</i>.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"A 'conovenomic' analysis of the milked venom from the mollusk-hunting cone snail <i>Conus textile</i>-The pharmacological importance of post-translational modifications","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2024-12-10 01:33:01.897972","timezone_type":1,"timezone":"+01:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"alpha-Conotoxin; Conopeptides; Conus textile; Mass spectrometry; Milkedvenom; Radula tooth; Post-translational modifications; nAChR","OtherDescriptors":null,"Notes":null,"AnaPub":2013,"MonPub":null,"DateUpdate":"2015-10-29","DateCreate":"2014-05-18","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000326941100020","VABBcode":null,"OpenAcc":0,"DOI":"10.1016/j.peptides.2013.09.004"},"refs":null,"anarec":{"AnaID":238150,"PubliDate":2013,"Pagination":"145-158","XtraPublOfAnaID":null,"ISBN":null,"Volume":"49","Issue":null,"BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":220987,"SerRR":"Peptides. 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