6oqp

Publication Abstract from PubMed

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 (1)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.

Structural and functional characterisation of a novel peptide from the Australian sea anemone Actinia tenebrosa.,Elnahriry KA, Wai DCC, Krishnarjuna B, Badawy NN, Chittoor B, MacRaild CA, Williams-Noonan BJ, Surm JM, Chalmers DK, Zhang AH, Peigneur S, Mobli M, Tytgat J, Prentis P, Norton RS Toxicon. 2019 Jul 11;168:104-112. doi: 10.1016/j.toxicon.2019.07.002. PMID:31302115^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.