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Structural and functional characterisation of a novel peptide from the Australian sea anemone Actinia tenebrosa
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. (2019). Structural and functional characterisation of a novel peptide from the Australian sea anemone Actinia tenebrosa. Toxicon 168: 104-112. https://dx.doi.org/10.1016/j.toxicon.2019.07.002
In: Toxicon. Elsevier: Oxford. ISSN 0041-0101; e-ISSN 1879-3150, meer
Peer reviewed article  
Beschikbaar in  Auteurs 
Trefwoorden
    Actinia tenebrosa Farquhar, 1898 [WoRMS]
    Marien/Kust
Author keywords
    Sea anemone; Cysteine-containing peptide; Structure; NMR spectroscopy;Lipid interactions
Auteurs  Top 
  • 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.
Abstract
    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 Actinia tenebrosa 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 1H 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.
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