mapping protein–protein interactions of the resistance-related bacterial zeta toxin–epsilon antitoxin complex (ε2ζ2) with high affinity peptide ligands using fluorescence polarization
Clicks: 278
ID: 247767
2016
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This
article has not been analysed, so there is no overall score —
reader engagement is measured and shown alongside.
Reader Engagement
Steady Performance
30.0
/100
278 views
27 readers
AI Quality Assessment
Not analyzed
Readership in this journal
SteadyRanked #117 of 300 articles by views in matec web of conferences
Most read
Least read
Bar heights use a square-root scale. Only the 120 most-read articles are drawn; the journal has 300 in total.
Mint this article as an NFT
Not yet mintedCreate a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.
5
SUSD
one-off · no wallet required
Abstract
Toxin–antitoxin systems constitute a native survival strategy of pathogenic bacteria and thus are potential targets of antibiotic drugs. Here, we target the Zeta–Epsilon toxin–antitoxin system, which is responsible for the stable maintenance of certain multiresistance plasmids in Gram-positive bacteria. Peptide ligands were designed on the basis of the ε2ζ2 complex. Three α helices of Zeta forming the protein–protein interaction (PPI) site were selected and peptides were designed conserving the residues interacting with Epsilon antitoxin while substituting residues binding intramolecularly to other parts of Zeta. Designed peptides were synthesized with an N-terminal fluoresceinyl-carboxy-residue for binding assays and provided active ligands, which were used to define the hot spots of the ε2ζ2 complex. Further shortening and modification of the binding peptides provided ligands with affinities <100 nM, allowing us to determine the most relevant PPIs and implement a robust competition binding assay.
| Reference Key |
fernndez-bachiller2016toxinsmapping
Use this key to autocite in the manuscript while using
SciMatic Manuscript Manager or Thesis Manager
|
|---|---|
| Authors | ;María Isabel Fernández-Bachiller;Iwona Brzozowska;Norbert Odolczyk;Urszula Zielenkiewicz;Piotr Zielenkiewicz;Jörg Rademann |
| Journal | matec web of conferences |
| Year | 2016 |
| DOI |
10.3390/toxins8070222
|
| URL | |
| Keywords |
Citations
No citations found. To add a citation, contact the admin at info@scimatic.org
Comments
No comments yet. Be the first to comment on this article.