<?xml version="1.0"?>
<oai_dc:dc xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:title>Antibacterial and leishmanicidal activities of temporin-SHd, a 17-residue long membrane-damaging peptide</dc:title>
  <dc:creator>Abbassi, F.</dc:creator>
  <dc:creator>Raja, Z.</dc:creator>
  <dc:creator>/Oury, Bruno</dc:creator>
  <dc:creator>/Gazanion, Elodie</dc:creator>
  <dc:creator>Piesse, C.</dc:creator>
  <dc:creator>/Sereno, Denis</dc:creator>
  <dc:creator>Nicolas, P.</dc:creator>
  <dc:creator>Foulon, T.</dc:creator>
  <dc:creator>Ladram, A.</dc:creator>
  <dc:subject>Antimicrobial peptide</dc:subject>
  <dc:subject>Amphibian</dc:subject>
  <dc:subject>Temporin-SH</dc:subject>
  <dc:subject>Circular dichroism</dc:subject>
  <dc:subject>Membrane interaction/permeabilization</dc:subject>
  <dc:subject>Antiparasitic activity</dc:subject>
  <dc:description>Temporins are a family of short antimicrobial peptides (8-17 residues) that mostly show potent activity against Gram-positive bacteria. Herein, we demonstrate that temporin-SHd, a 17-residue peptide with a net charge of +2 (FLPAALAGIGGILGKLF(amide)) expressed a broad spectrum of antimicrobial activity. This peptide displayed potent antibacterial activities against Gram-negative and Gram-positive bacteria, including multi-drug resistant Staphylococcus aureus strains, as well as antiparasitic activity against promastigote and the intracellular stage (amastigote) of Leishmania infantum, at concentration not toxic for the macrophages. Temporin-SHd that is structured in a non-amphipathic alpha-helix in anionic membrane-mimetic environments, strongly and selectively perturbs anionic bilayer membranes by interacting with the polar head groups and acyl region of the phospholipids, with formation of regions of two coexisting phases: one phase rich in peptide and the other lipid-rich. The disruption of lipid packing within the bilayer may lead to the formation of transient pores and membrane permeation/disruption once a threshold peptide accumulation is reached. To our knowledge, Temporin-SHd represents the first known 17-residue long temporin expressing such broad spectrum of antimicrobial activity including members of the trypanosomatidae family. Additionally, since only a few shorter members (13 residues) of the temporin family are known to display antileishmanial activity (temporins-TA, -TB and -SHa), SHd is an interesting tool to analyze the antiparasitic mechanism of action of temporins.</dc:description>
  <dc:date>2013</dc:date>
  <dc:type>text</dc:type>
  <dc:identifier>https://www.documentation.ird.fr/hor/fdi:010060735</dc:identifier>
  <dc:identifier>fdi:010060735</dc:identifier>
  <dc:identifier>Abbassi F., Raja Z., Oury Bruno, Gazanion Elodie, Piesse C., Sereno Denis, Nicolas P., Foulon T., Ladram A.. Antibacterial and leishmanicidal activities of temporin-SHd, a 17-residue long membrane-damaging peptide. 2013, 95 (2),  388-399</dc:identifier>
  <dc:language>EN</dc:language>
</oai_dc:dc>
