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Copper-binding motifs Xxx-His or Xxx-Zzz-His (ATCUN) linked to an antimicrobial peptide: Cu-binding, antimicrobial activity and ROS production

Journal of inorganic biochemistry, 2020-12, Vol.213 [Peer Reviewed Journal]

Distributed under a Creative Commons Attribution 4.0 International License ;ISSN: 0162-0134 ;EISSN: 1873-3344 ;DOI: 10.1016/j.jinorgbio.2020.111255

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  • Title:
    Copper-binding motifs Xxx-His or Xxx-Zzz-His (ATCUN) linked to an antimicrobial peptide: Cu-binding, antimicrobial activity and ROS production
  • Author: Bouraguba, Merwan ; Glattard, Elise ; Naudé, Maxime ; Pelletier, Rémi ; Aisenbrey, Christopher ; Bechinger, Burkhard ; Raibaut, Laurent ; Lebrun, Vincent ; Faller, Peter
  • Subjects: Chemical Sciences ; Coordination chemistry ; Medicinal Chemistry
  • Is Part Of: Journal of inorganic biochemistry, 2020-12, Vol.213
  • Description: Depending on the coordination, copper ions can have a very high activity in catalyzing the production of reactive oxygen species. Thus interest arose in increasing the activity of antimicrobial peptides (AMPs) by equipping them with a Cu-binding unit. Several examples, native and engineered, have been investigated with the motif Xxx-Zzz-His, called Amino Terminal Cu(II)- and Ni(II)-binding (ATCUN) motif. Here we investigate a short AMP that was equipped either with Xxx-Zzz-His or Xxx-His. Xxx-His is a shorter motif and yields a more redox active copper complex. The control AMP, Xxx-His-AMP and Xxx-Zzz-His-AMP were investigated toward Cu-binding, Reactive Oxygen Species (ROS) production and antimicrobial activity in E. coli. The data indicate that these Cu-binding motifs have very limited impact on antimicrobial activity and low ROS production capability.
  • Publisher: Elsevier
  • Language: English
  • Identifier: ISSN: 0162-0134
    EISSN: 1873-3344
    DOI: 10.1016/j.jinorgbio.2020.111255
  • Source: Hyper Article en Ligne (HAL) (Open Access)
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