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    • Fulltext

       

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      Permanent link:
      https://www.ias.ac.in/article/fulltext/jbsc/036/05/0781-0791

    • Keywords

       

      Actinoporin; hemolytic peptide; permeabilizing activity; pore-forming toxin; sticholysin

    • Abstract

       

      The sea anemone Stichodactyla helianthus produces two pore-forming proteins, sticholysins I and II (St I and St II). Despite their high identity (93%), these toxins exhibit differences in hemolytic activity that can be related to those found in their N-terminal. To clarify the contribution of the N-terminal amino acid residues to the activity of the toxins, we synthesized peptides spanning residues 1–31 of St I (StI1-31) or 1–30 of St II (StII1-30) and demonstrated that StII1-30 promotes erythrocyte lysis to a higher extent than StI1-31. For a better understanding of the molecular mechanism underlying the peptide activity, here we studied their binding to lipid monolayers and pemeabilizing activity in liposomes. For this, we examined the effect on peptide membranotropic activity of including phospatidic acid and cholesterol in a lipid mixture of phosphatidylcholine and sphingomyelin. The results suggest the importance of continuity of the 1–10 hydrophobic sequence in StII1-30 for displaying higher binding and activity, in spite of both peptides’ abilities to form pores in giant unilamellar vesicles. Thus, the different peptide membranotropic action is explained in terms of the differences in hydrophobic and electrostatic peptide properties as well as the enhancing role of membrane inhomogeneities.

    • Author Affiliations

       

      Uris Ros1 Lohans Pedrera1 Daylín Díaz1 Juan C De Karam1 Tatiane P Sudbrack2 Pedro A Valiente1 Diana Martínez1 Eduardo M Cilli3 Fabiola Pazos1 Rosangela Itri2 Maria E Lanio1 Shirley Schreier4 Carlos Álvarez1

      1. Center for Protein Studies, Biology Faculty, University of Havana, Havana, Cuba
      2. Department of Applied Physics, Institute of Physics, University of São Paulo, São Paulo, Brazil
      3. Department of Biochemistry, Institute of Chemistry, São Paulo State University, Araraquara, São Paulo, Brazil
      4. Department of Biochemistry, Institute of Chemistry, University of São Paulo, São Paulo, Brazil

    • Dates

       
      Published
      December 2011
      Manuscript received
      7 June 2011
      Accepted
      17 August 2011
      Early published
      29 October 2011

  • Journal of Biosciences | News

      Forthcoming Special issue.


    • To trigger further research on plant mitochondria, the Journal of Biosciences is bringing out a special issue titled "Plant Mitochondria: Properties and Interactions with Other Organelles".


      Plant mitochondria are quite distinct and have unique features, such as a cyanide-insensitive alternate pathway. They also interact with chloroplasts to optimize photosynthetic carbon assimilation.


      Submissions are welcome until 30 July 2023. The contributions can be original articles, short communications, reviews, or mini-reviews on any topic related to plant mitochondria.


      Authors can submit their articles online at https://www.editorialmanager.com/jbsc/default2.aspx

      Posted on April 12, 2023
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      Posted on July 25, 2019

      Click here for Editorial Note on CAP Mode

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