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@ARTICLE{Ros:127406,
      author       = {U. Ros and W. Rodríguez-Vera and L. Pedrera and P. A.
                      Valiente and S. Cabezas and M. E. Lanio and A. J.
                      García-Sáez$^*$ and C. Alvarez},
      title        = {{D}ifferences in activity of actinoporins are related with
                      the hydrophobicity of their {N}-terminus.},
      journal      = {Biochimie},
      volume       = {116},
      issn         = {0300-9084},
      address      = {Paris [u.a.]},
      publisher    = {Elsevier},
      reportid     = {DKFZ-2017-03429},
      pages        = {70 - 78},
      year         = {2015},
      abstract     = {Actinoporins are pore-forming toxins (PFT) produced by sea
                      anemones with molecular mass around 20 kDa and high affinity
                      for sphingomyelin. The most studied atinoporins are
                      sticholysins I and II (StI/StII) from Stichodactyla
                      helianthus, equinatoxin II (EqtII) from Actinia equina, and
                      fragaceatoxin C (FraC) from Actinia fragacea. Their
                      N-terminal sequences encompassing residues 1-30 seem to be
                      the best candidates for pore formation. This segment
                      comprises an amphipathic α-helix preceded by a more or less
                      hydrophobic segment, depending on the toxin, of around 10
                      amino acid residues. Although it is clear that the
                      N-terminal is the most variable sequence in this protein
                      family, the role of their hydrophobic segment in not fully
                      understood. Here we show a comparison of StI, StII, EqtII,
                      and FraC activities with that of their respective N-terminal
                      synthetic peptides. The hemolytic and permeabilizing
                      activity of the peptides reproduce qualitatively the
                      behavior of their respective parental proteins and are
                      particularly related to the hydrophobicity of the
                      corresponding 1-10 segment. Furthermore, the dendrogram
                      analysis of actinoporins' N-terminal sequence allows
                      relating differences in alignment with differences in
                      activity among the four toxins. We have also evaluated the
                      penetration depth of the N-terminal segment of StI and StII
                      by using Trp-containing peptide-analogs. Our data suggest
                      that the N-terminus of StII is more deeply buried into the
                      hydrophobic core of the bilayer than that of StI. We
                      hypothesize that the highest activity of StII could be
                      ascribed to a larger hydrophobic continuum, an uninterrupted
                      sequence of non-charged mainly hydrophobic amino acid
                      residues, of its N-terminus promoting a highest ability to
                      partially insert in the membrane core. Moreover, as we show
                      for four related peptides that a higher hydrophobicity
                      contributes to increase the activity, we reinforce the
                      notion that this property must be taken into account to
                      design new potent membranotropic agents.},
      keywords     = {Peptides (NLM Chemicals)},
      cin          = {B160},
      ddc          = {540},
      cid          = {I:(DE-He78)B160-20160331},
      pnm          = {312 - Functional and structural genomics (POF3-312)},
      pid          = {G:(DE-HGF)POF3-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:26134716},
      doi          = {10.1016/j.biochi.2015.06.024},
      url          = {https://inrepo02.dkfz.de/record/127406},
}