Blog
About

94
views
0
recommends
+1 Recommend
0 collections
    4
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      An unusual peptide from Conus villepinii: synthesis, solution structure, and cardioactivity.

      Read this article at

      ScienceOpenPublisherPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          The venom of marine cone snails contains a variety of conformationally constrained peptides utilized by the animal to capture prey. Besides numerous conotoxins, which are characterized by complex disulfide patterns, other peptides with only a single disulfide bridge were isolated from different conus species. Here, we report the synthesis, structure elucidation and biological evaluation of the novel C-terminally amidated decapeptide CCAP-vil, PFc[CNSFGC]YN-NH(2), from Conus villepinii. The linear precursor peptide was generated by standard solid phase synthesis. Oxidation of the cysteine residues to yield the disulfide-bridged peptide was investigated under different conditions, including several ionic liquids (ILs) as new biocompatible reaction media. Among the examined ILs, 1-ethyl-3-methylimidazolium tosylate ([C(2)mim][OTs]) was most efficient for CCAP-vil oxidative folding, since oxidation occurred without any byproduct formation. The structure of CCAP-vil was determined by NMR methods in aqueous solution and revealed a loop structure adopting a type(I) beta-turn between residues 4-7 imposed by the flanking disulfide bridge. The amino acid side chains of Pro(1), Phe(2), Phe(6) and Tyr(9) point in three directions away from the cyclic core into the solvent creating a rather hydrophobic surface of the molecule. Based on sequence homology to cardioactive peptides (CAPs) from gastropods and arthropods, such as PFc[CNAFTGC]-NH(2) (CCAP), the influence of CCAP-vil on heart rate using zebrafish embryos was investigated. CCAP-vil reduced the heart rate immediately upon injection into the heart as well as upon indirect application indicating an opposite effect to the cardioaccelerating CCAP.

          Related collections

          Author and article information

          Journal
          Peptides
          Peptides
          Elsevier BV
          1873-5169
          0196-9781
          Jul 2010
          : 31
          : 7
          Affiliations
          [1 ] Center for Molecular Biomedicine, Department of Biochemistry, Peptide Chemistry Group, Friedrich Schiller University, Hans-Knöll-Strasse 2, D-07745 Jena, Germany.
          Article
          S0196-9781(10)00154-3
          10.1016/j.peptides.2010.04.002
          20385188

          Comments

          Comment on this article