@article{fdi:010060735,
  title = {{A}ntibacterial and leishmanicidal activities of temporin-{SH}d, a 17-residue long membrane-damaging peptide},
  author = {{A}bbassi, {F}. and {R}aja, {Z}. and {O}ury, {B}runo and {G}azanion, {E}lodie and {P}iesse, {C}. and {S}ereno, {D}enis and {N}icolas, {P}. and {F}oulon, {T}. and {L}adram, {A}.},
  editor = {},
  language = {{ENG}},
  abstract = {{T}emporins are a family of short antimicrobial peptides (8-17 residues) that mostly show potent activity against {G}ram-positive bacteria. {H}erein, we demonstrate that temporin-{SH}d, a 17-residue peptide with a net charge of +2 ({FLPAALAGIGGILGKLF}(amide)) expressed a broad spectrum of antimicrobial activity. {T}his peptide displayed potent antibacterial activities against {G}ram-negative and {G}ram-positive bacteria, including multi-drug resistant {S}taphylococcus aureus strains, as well as antiparasitic activity against promastigote and the intracellular stage (amastigote) of {L}eishmania infantum, at concentration not toxic for the macrophages. {T}emporin-{SH}d 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. {T}he 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. {T}o our knowledge, {T}emporin-{SH}d represents the first known 17-residue long temporin expressing such broad spectrum of antimicrobial activity including members of the trypanosomatidae family. {A}dditionally, since only a few shorter members (13 residues) of the temporin family are known to display antileishmanial activity (temporins-{TA}, -{TB} and -{SH}a), {SH}d is an interesting tool to analyze the antiparasitic mechanism of action of temporins.},
  keywords = {{A}ntimicrobial peptide ; {A}mphibian ; {T}emporin-{SH} ; {C}ircular dichroism ; {M}embrane interaction/permeabilization ; {A}ntiparasitic activity},
  booktitle = {},
  journal = {{B}iochimie},
  volume = {95},
  numero = {2},
  pages = {388--399},
  ISSN = {0300-9084},
  year = {2013},
  DOI = {10.1016/j.biochi.2012.10.015},
  URL = {https://www.documentation.ird.fr/hor/fdi:010060735},
}