{"refrec":{"BRefID":322938,"RR":"<b>Elnahriry, K.A.; Wai, D.C.C.; Krishnarjuna, B.; Badawy, N.N.; Chittoor, B.; MacRaild, C.A.; Williams-Noonan, B.J.; Surm, J.M.; Chalmers, D.K.; Zhang, A.H.; Peigneur, S.; Mobli, M.; Tytgat, J.; Prentis, P.; Norton, R.S.</b> (2019). Structural and functional characterisation of a novel peptide from the Australian sea anemone <i>Actinia tenebrosa</i>. <i>Toxicon 168</i>: 104-112. <a href=\"https://dx.doi.org/10.1016/j.toxicon.2019.07.002\" target=\"_blank\">https://dx.doi.org/10.1016/j.toxicon.2019.07.002</a>","BEntID":316409,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>Toxicon 168</i>: 104-112. <a href=\"https://dx.doi.org/10.1016/j.toxicon.2019.07.002\" target=\"_blank\">https://dx.doi.org/10.1016/j.toxicon.2019.07.002</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Elnahriry, K.A.; Wai, D.C.C.; Krishnarjuna, B.; Badawy, N.N.; Chittoor, B.; MacRaild, C.A.; Williams-Noonan, B.J.; Surm, J.M.; Chalmers, D.K.; Zhang, A.H.; Peigneur, S.; Mobli, M.; Tytgat, J.; Prentis, P.; Norton, R.S.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Elnahriry, K.A. <i>et al.</i>","Englishabstract":"Sea anemone venoms have long been recognised as a rich source of peptides with interesting pharmacological and structural properties. Our recent transcriptomic studies of the Australian sea anemone <em>Actinia tenebrosa</em> have identified a novel 13-residue peptide, U-AITx-Ate1. U-AITx-Ate1 contains a single disulfide bridge and bears no significant homology to previously reported amino acid sequences of peptides from sea anemones or other species. We have produced U-AITx-Ate1 using solid-phase peptide synthesis, followed by oxidative folding and purification of the folded peptide using reversed-phase high-performance liquid chromatography. The solution structure of U-AITx-Ate1 was determined based on two-dimensional nuclear magnetic resonance spectroscopic data. Diffusion-ordered NMR spectroscopy revealed that U-AITx-Ate1 was monomeric in solution. Perturbations in the 1D <sup>1</sup>H NMR spectrum of U-AITx-Ate1 in the presence of dodecylphosphocholine micelles together with molecular dynamics simulations indicated an interaction of U-AITx-Ate1 with lipid membranes, although no binding was detected to 100% POPC and 80% POPC: 20% POPG lipid nanodiscs by isothermal titration calorimetry. Functional assays were performed to explore the biological activity profile of U-AITx-Ate1. U-AITx-Ate1 showed no activity in voltage-clamp electrophysiology assays and no change in behaviour and mortality rates in crustacea. Moderate cytotoxic activity was observed against two breast cancer cell lines.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Structural and functional characterisation of a novel peptide from the Australian sea anemone <i>Actinia tenebrosa</i>","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":"Sea anemone; Cysteine-containing peptide; Structure; NMR spectroscopy;Lipid interactions","OtherDescriptors":null,"Notes":null,"AnaPub":2019,"MonPub":null,"DateUpdate":"2020-04-14","DateCreate":"2020-04-07","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000484876000015","VABBcode":null,"OpenAcc":0,"DOI":"10.1016/j.toxicon.2019.07.002"},"refs":null,"anarec":{"AnaID":322938,"PubliDate":2019,"Pagination":"104-112","XtraPublOfAnaID":null,"ISBN":null,"Volume":"168","Issue":null,"BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":43961,"SerRR":"Toxicon. 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