{"refrec":{"BRefID":307950,"RR":"<b>Sunanda, P.; Krishnarjuna, B.; Peigneur, S.; Mitchell, M.L.; Estrada, R.; Villegas-Moreno, J.; Pennington, M.W.; Tytgat, J.; Norton, R.S.</b> (2018). Identification, chemical synthesis, structure, and function of a new K<sub>V</sub>1 channel blocking peptide from <i>Oulactis</i> sp. <i>Peptide Science 110(4)</i>: e24073. <a href=\"https://dx.doi.org/10.1002/pep2.24073\" target=\"_blank\">https://dx.doi.org/10.1002/pep2.24073</a>","BEntID":300276,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":0,"RefStringPartII":" <i>Peptide Science 110(4)</i>: e24073. <a href=\"https://dx.doi.org/10.1002/pep2.24073\" target=\"_blank\">https://dx.doi.org/10.1002/pep2.24073</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Sunanda, P.; Krishnarjuna, B.; Peigneur, S.; Mitchell, M.L.; Estrada, R.; Villegas-Moreno, J.; Pennington, M.W.; Tytgat, J.; Norton, R.S.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Sunanda, P. <i>et al.</i>","Englishabstract":"Rapid progress in transcriptomic and proteomic studies of sea anemones has led to the identification of a large number of new peptide sequences. Some of these peptides have high sequence similarity and identical cysteine frameworks to those of previously reported sequences. One such peptide we have identified from a transcriptomic study of <i>Oulactis</i> sp is OspTx2a, which has a cysteine framework similar to that of ShK (from <i>Stichodactyla helianthus</i>) and BgK (from <i>Bunodosoma granulifera</i>). This peptide was made using solid‐phase peptide synthesis, but, upon oxidative folding, it generated two peptides with identical masses (OspTx2a‐p1 and OspTx2a‐p2) that were distinguishable by high‐performance liquid chromatography. The structures of OspTx2a‐p1 and OspTx2a‐p2 were determined using nuclear magnetic resonance spectroscopy, and voltage‐clamp electrophysiology assays were performed in order to assess the activity against a range of potassium channels. The structures of the two peptides were very similar to each other and to BgK, with the same disulfide bond connectivities, and both had an all‐<i>trans</i> backbone conformation. In functional assays, both OspTx2a‐p1 and OspTx2a‐p2 inhibited K<sub>V</sub>1.2 and K<sub>V</sub>1.6 channel currents at low µM concentrations, with similar but not identical IC<sub>50</sub> values. Peptides containing a C‐terminal Cys residue are particularly sensitive to racemization at this residue, and the two products obtained for OspTx2a could be a consequence of racemization of the Cys residue at its C‐terminus during synthesis. NMR chemical shift differences between the two products and their structural preferences for a <span class=\"smallCaps\">d</span>‐Cys residue were consistent with this interpretation.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Identification, chemical synthesis, structure, and function of a new K<sub>V</sub>1 channel blocking peptide from <i>Oulactis</i> sp.","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2024-12-10 01:33:17.368041","timezone_type":1,"timezone":"+01:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"cysteine-rich peptide; isomers; K-V channel; NMR spectroscopy; OspTx2a;sea anemone; structure","OtherDescriptors":null,"Notes":null,"AnaPub":2018,"MonPub":null,"DateUpdate":"2019-03-18","DateCreate":"2019-03-13","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000443404400004","VABBcode":null,"OpenAcc":0,"DOI":"10.1002/pep2.24073"},"refs":null,"anarec":{"AnaID":307950,"PubliDate":2018,"Pagination":"e24073","XtraPublOfAnaID":null,"ISBN":null,"Volume":"110","Issue":"4","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":308686,"SerRR":"Peptide Science. 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